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data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184832/Stabilization_of_acidified_milk_drinks_using_pectin"><img alt="Research paper thumbnail of Stabilization of acidified milk drinks using pectin" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184832/Stabilization_of_acidified_milk_drinks_using_pectin">Stabilization of acidified milk drinks using pectin</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The present study was carried out based on a special capacity of high methoxyl pectin in stabiliz...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The present study was carried out based on a special capacity of high methoxyl pectin in stabilizing acidified milk drinks. The presence of an optimal concentration of high methoxyl pectin can prevent the defects of acidified milk drinks such as protein flocculation, sedimentation and macroscopic wheying-off. A narrow range of pectin including 0, 0.1, 0.15, 0.2, 0.25, 0.3, and 0.4%</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184832"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184832"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184832; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184832]").text(description); $(".js-view-count[data-work-id=18184832]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184832; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184832']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184832, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184832]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184832,"title":"Stabilization of acidified milk drinks using pectin","translated_title":"","metadata":{"abstract":"The present study was carried out based on a special capacity of high methoxyl pectin in stabilizing acidified milk drinks. 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184797"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184797/Effect_of_high_pressure_on_aggregation_and_thermal_gelation_of_%CE%B2_lactoglobulin"><img alt="Research paper thumbnail of Effect of high pressure on aggregation and thermal gelation of β-lactoglobulin" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184797/Effect_of_high_pressure_on_aggregation_and_thermal_gelation_of_%CE%B2_lactoglobulin">Effect of high pressure on aggregation and thermal gelation of β-lactoglobulin</a></div><div class="wp-workCard_item"><span>Milchwissenschaft</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Solutions containing 5% purified β-Lg B at pH 7.5 were subjected to high pressure treatments of v...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Solutions containing 5% purified β-Lg B at pH 7.5 were subjected to high pressure treatments of varying intensity and duration. The state of aggregation and the thermal gelation properties of the pressure-treated samples were monitored immediately after depressurization and after storage for 24 h at 5°C. A pressure of 150 MPa applied for 30 min or pressures in excess of 300 MPa applied for 0 or 30 min led to formation of soluble aggregates. When continued for 30 min, a pressure of 450 MPa caused gelation of the 5% β-Lg solution. The state of aggregation of the protein changed over time, generally with an increasing proportion of polymers. For samples measured after 24 h of storage a good inverse correlation was found between pressure intensity, proportion of polymers and thermal gelation properties. With increasing pressure, the time of gelation increased and the total gel stiffness decreased.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184797"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184797"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184797; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184797]").text(description); $(".js-view-count[data-work-id=18184797]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184797; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184797']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184797, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184797]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184797,"title":"Effect of high pressure on aggregation and thermal gelation of β-lactoglobulin","translated_title":"","metadata":{"abstract":"Solutions containing 5% purified β-Lg B at pH 7.5 were subjected to high pressure treatments of varying intensity and duration. The state of aggregation and the thermal gelation properties of the pressure-treated samples were monitored immediately after depressurization and after storage for 24 h at 5°C. A pressure of 150 MPa applied for 30 min or pressures in excess of 300 MPa applied for 0 or 30 min led to formation of soluble aggregates. When continued for 30 min, a pressure of 450 MPa caused gelation of the 5% β-Lg solution. The state of aggregation of the protein changed over time, generally with an increasing proportion of polymers. For samples measured after 24 h of storage a good inverse correlation was found between pressure intensity, proportion of polymers and thermal gelation properties. With increasing pressure, the time of gelation increased and the total gel stiffness decreased.","publication_name":"Milchwissenschaft"},"translated_abstract":"Solutions containing 5% purified β-Lg B at pH 7.5 were subjected to high pressure treatments of varying intensity and duration. The state of aggregation and the thermal gelation properties of the pressure-treated samples were monitored immediately after depressurization and after storage for 24 h at 5°C. A pressure of 150 MPa applied for 30 min or pressures in excess of 300 MPa applied for 0 or 30 min led to formation of soluble aggregates. When continued for 30 min, a pressure of 450 MPa caused gelation of the 5% β-Lg solution. The state of aggregation of the protein changed over time, generally with an increasing proportion of polymers. For samples measured after 24 h of storage a good inverse correlation was found between pressure intensity, proportion of polymers and thermal gelation properties. With increasing pressure, the time of gelation increased and the total gel stiffness decreased.","internal_url":"https://www.academia.edu/18184797/Effect_of_high_pressure_on_aggregation_and_thermal_gelation_of_%CE%B2_lactoglobulin","translated_internal_url":"","created_at":"2015-11-12T00:16:18.026-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Effect_of_high_pressure_on_aggregation_and_thermal_gelation_of_β_lactoglobulin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184795"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184795/Formation_of_nanotubes_and_gels_at_a_broad_pH_range_upon_partial_hydrolysis_of_bovine_%CE%B1_lactalbumin"><img alt="Research paper thumbnail of Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184795/Formation_of_nanotubes_and_gels_at_a_broad_pH_range_upon_partial_hydrolysis_of_bovine_%CE%B1_lactalbumin">Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin</a></div><div class="wp-workCard_item"><span>International Dairy Journal</span><span>, 2015</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184795"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184795"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184795; 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dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184795]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184795,"title":"Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin","translated_title":"","metadata":{"publication_date":{"day":null,"month":null,"year":2015,"errors":{}},"publication_name":"International Dairy Journal"},"translated_abstract":null,"internal_url":"https://www.academia.edu/18184795/Formation_of_nanotubes_and_gels_at_a_broad_pH_range_upon_partial_hydrolysis_of_bovine_%CE%B1_lactalbumin","translated_internal_url":"","created_at":"2015-11-12T00:16:17.902-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Formation_of_nanotubes_and_gels_at_a_broad_pH_range_upon_partial_hydrolysis_of_bovine_α_lactalbumin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":181926,"name":"Dairy","url":"https://www.academia.edu/Documents/in/Dairy"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184793"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184793/Pilot_scale_purification_of_%CE%B1_lactalbumin_from_enriched_whey_protein_concentrate_by_anion_exchange_chromatography_and_ultrafiltration"><img alt="Research paper thumbnail of Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184793/Pilot_scale_purification_of_%CE%B1_lactalbumin_from_enriched_whey_protein_concentrate_by_anion_exchange_chromatography_and_ultrafiltration">Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration</a></div><div class="wp-workCard_item"><span>Dairy Science & Technology</span><span>, 2015</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT A method based on anion exchange chromatography (AIEX) in combination with ultrafiltrati...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">ABSTRACT A method based on anion exchange chromatography (AIEX) in combination with ultrafiltration (UF) was developed to obtain kilogram-scale amounts of bovine α-lactalbumin (α-La) of high purity from α-La-enriched whey protein concentrate (αWPC). Initially, α-La was successfully purified, at laboratory scale, from a 10% solution of αWPC. Removal of casein and denatured whey protein by acid precipitation resulted in a α-La purity of 78%. A further purification by AIEX eluting with sodium acetate (NaAc) buffer led to a final purity and recovery of 100 and 85%, respectively. Based on this, the process was simplified and optimized for pilot-scale purification by selective binding of β-lactoglobulin (β-Lg). Batchwise expanded bed AIEX using a column with 5 L of Q Sepharose matrix was performed. Pure α-La was obtained in the run through buffer. In the end, 1100 g of holo form α-La was obtained with a purity of 97.4% in protein and a recovery of 80%, calculated based on the protein detectable in reversed phase high-performance liquid chromatography (RP-HPLC). Thus, by combining AIEX and UF, heating was avoided allowing production of α-La in kilo-scale with high purity and recovery from αWPC with a minimum volume of buffer solutions.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184793"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184793"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184793; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184793]").text(description); $(".js-view-count[data-work-id=18184793]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184793; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184793']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184793, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184793]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184793,"title":"Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration","translated_title":"","metadata":{"abstract":"ABSTRACT A method based on anion exchange chromatography (AIEX) in combination with ultrafiltration (UF) was developed to obtain kilogram-scale amounts of bovine α-lactalbumin (α-La) of high purity from α-La-enriched whey protein concentrate (αWPC). Initially, α-La was successfully purified, at laboratory scale, from a 10% solution of αWPC. Removal of casein and denatured whey protein by acid precipitation resulted in a α-La purity of 78%. A further purification by AIEX eluting with sodium acetate (NaAc) buffer led to a final purity and recovery of 100 and 85%, respectively. Based on this, the process was simplified and optimized for pilot-scale purification by selective binding of β-lactoglobulin (β-Lg). Batchwise expanded bed AIEX using a column with 5 L of Q Sepharose matrix was performed. Pure α-La was obtained in the run through buffer. In the end, 1100 g of holo form α-La was obtained with a purity of 97.4% in protein and a recovery of 80%, calculated based on the protein detectable in reversed phase high-performance liquid chromatography (RP-HPLC). Thus, by combining AIEX and UF, heating was avoided allowing production of α-La in kilo-scale with high purity and recovery from αWPC with a minimum volume of buffer solutions.","publication_date":{"day":null,"month":null,"year":2015,"errors":{}},"publication_name":"Dairy Science \u0026 Technology"},"translated_abstract":"ABSTRACT A method based on anion exchange chromatography (AIEX) in combination with ultrafiltration (UF) was developed to obtain kilogram-scale amounts of bovine α-lactalbumin (α-La) of high purity from α-La-enriched whey protein concentrate (αWPC). Initially, α-La was successfully purified, at laboratory scale, from a 10% solution of αWPC. Removal of casein and denatured whey protein by acid precipitation resulted in a α-La purity of 78%. A further purification by AIEX eluting with sodium acetate (NaAc) buffer led to a final purity and recovery of 100 and 85%, respectively. Based on this, the process was simplified and optimized for pilot-scale purification by selective binding of β-lactoglobulin (β-Lg). Batchwise expanded bed AIEX using a column with 5 L of Q Sepharose matrix was performed. Pure α-La was obtained in the run through buffer. In the end, 1100 g of holo form α-La was obtained with a purity of 97.4% in protein and a recovery of 80%, calculated based on the protein detectable in reversed phase high-performance liquid chromatography (RP-HPLC). Thus, by combining AIEX and UF, heating was avoided allowing production of α-La in kilo-scale with high purity and recovery from αWPC with a minimum volume of buffer solutions.","internal_url":"https://www.academia.edu/18184793/Pilot_scale_purification_of_%CE%B1_lactalbumin_from_enriched_whey_protein_concentrate_by_anion_exchange_chromatography_and_ultrafiltration","translated_internal_url":"","created_at":"2015-11-12T00:16:17.789-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Pilot_scale_purification_of_α_lactalbumin_from_enriched_whey_protein_concentrate_by_anion_exchange_chromatography_and_ultrafiltration","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":60,"name":"Mechanical Engineering","url":"https://www.academia.edu/Documents/in/Mechanical_Engineering"},{"id":42955,"name":"Dairy Science and Technology","url":"https://www.academia.edu/Documents/in/Dairy_Science_and_Technology"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184791"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184791/Emulsifying_salt_increase_stability_of_cheese_emulsions_during_holding"><img alt="Research paper thumbnail of Emulsifying salt increase stability of cheese emulsions during holding" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184791/Emulsifying_salt_increase_stability_of_cheese_emulsions_during_holding">Emulsifying salt increase stability of cheese emulsions during holding</a></div><div class="wp-workCard_item"><span>LWT - Food Science and Technology</span><span>, 2015</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT In cheese powder production, cheese is mixed and melted with water and emulsifying salt ...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">ABSTRACT In cheese powder production, cheese is mixed and melted with water and emulsifying salt to form an emulsion (cheese feed) which is required to remain stable at 60 °C for 1 h and during further processing until spray drying. Addition of emulsifying salts ensures this, but recent demands for reduction of sodium and phosphate in foods makes production of cheese powder without or with minimal amounts of emulsifying salts desirable. The present work uses a centrifugation method to characterize stability of model cheese feeds. Stability of cheese feed with emulsifying salt increased with holding time at 60 °C, especially when no stirring was applied. No change in stability during holding was observed in cheese feeds without emulsifying salt. This effect is suggested to be due to continued exerted functionality of the emulsifying salt, possibly through reorganizations of the mineral balance.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184791"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184791"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184791; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184791]").text(description); $(".js-view-count[data-work-id=18184791]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184791; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184791']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184791, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184791]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184791,"title":"Emulsifying salt increase stability of cheese emulsions during holding","translated_title":"","metadata":{"abstract":"ABSTRACT In cheese powder production, cheese is mixed and melted with water and emulsifying salt to form an emulsion (cheese feed) which is required to remain stable at 60 °C for 1 h and during further processing until spray drying. Addition of emulsifying salts ensures this, but recent demands for reduction of sodium and phosphate in foods makes production of cheese powder without or with minimal amounts of emulsifying salts desirable. The present work uses a centrifugation method to characterize stability of model cheese feeds. Stability of cheese feed with emulsifying salt increased with holding time at 60 °C, especially when no stirring was applied. No change in stability during holding was observed in cheese feeds without emulsifying salt. This effect is suggested to be due to continued exerted functionality of the emulsifying salt, possibly through reorganizations of the mineral balance.","publication_date":{"day":null,"month":null,"year":2015,"errors":{}},"publication_name":"LWT - Food Science and Technology"},"translated_abstract":"ABSTRACT In cheese powder production, cheese is mixed and melted with water and emulsifying salt to form an emulsion (cheese feed) which is required to remain stable at 60 °C for 1 h and during further processing until spray drying. Addition of emulsifying salts ensures this, but recent demands for reduction of sodium and phosphate in foods makes production of cheese powder without or with minimal amounts of emulsifying salts desirable. The present work uses a centrifugation method to characterize stability of model cheese feeds. Stability of cheese feed with emulsifying salt increased with holding time at 60 °C, especially when no stirring was applied. No change in stability during holding was observed in cheese feeds without emulsifying salt. This effect is suggested to be due to continued exerted functionality of the emulsifying salt, possibly through reorganizations of the mineral balance.","internal_url":"https://www.academia.edu/18184791/Emulsifying_salt_increase_stability_of_cheese_emulsions_during_holding","translated_internal_url":"","created_at":"2015-11-12T00:16:17.663-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Emulsifying_salt_increase_stability_of_cheese_emulsions_during_holding","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":29980,"name":"Animal Production","url":"https://www.academia.edu/Documents/in/Animal_Production"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184790"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184790/Using_Surface_Plasmon_Resonance_Technology_to_Screen_Interactions_Between_Exopolysaccharides_and_Milk_Proteins"><img alt="Research paper thumbnail of Using Surface Plasmon Resonance Technology to Screen Interactions Between Exopolysaccharides and Milk Proteins" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184790/Using_Surface_Plasmon_Resonance_Technology_to_Screen_Interactions_Between_Exopolysaccharides_and_Milk_Proteins">Using Surface Plasmon Resonance Technology to Screen Interactions Between Exopolysaccharides and Milk Proteins</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Surface plasmon resonance-based biosensors enable the interaction between biomolecules to be moni...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Surface plasmon resonance-based biosensors enable the interaction between biomolecules to be monitored in real time with a label-free assay format. In the present study, the technique was used to assess the interaction between exopolysaccharides (EPS) and different milk proteins. The EPS were derived from three homopolysaccharide (HoPS)-producing Lactobacilli strains; Lactobacillus sakei, Lactobacillus plantarum, and Lactobacillus salvarius. The purified milk proteins applied were β-casein, β-lactoglobulin, and κ-casein. The results show that the binding capacity depends on the pH and decreases with increasing pH. HoPS from L. salvarius and L. sakei provided the highest binding response and interacted with κ-casein at all the tested pH values, i.e. in the range 4.0−5.5, and with β-casein at pH 4.0−5.0. When examined at pH 4.0, only HoPS from L. salvarius and L. sakei interacted with β-lactoglobulin. Under the tested conditions, HoPS from L. plantarum showed always either a lower binding response or no binding at all compared with HoPS from L. salvarius and L. sakei.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184790"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184790"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184790; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184790]").text(description); $(".js-view-count[data-work-id=18184790]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184790; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184790']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184790, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184790]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184790,"title":"Using Surface Plasmon Resonance Technology to Screen Interactions Between Exopolysaccharides and Milk Proteins","translated_title":"","metadata":{"abstract":"Surface plasmon resonance-based biosensors enable the interaction between biomolecules to be monitored in real time with a label-free assay format. In the present study, the technique was used to assess the interaction between exopolysaccharides (EPS) and different milk proteins. The EPS were derived from three homopolysaccharide (HoPS)-producing Lactobacilli strains; Lactobacillus sakei, Lactobacillus plantarum, and Lactobacillus salvarius. The purified milk proteins applied were β-casein, β-lactoglobulin, and κ-casein. The results show that the binding capacity depends on the pH and decreases with increasing pH. HoPS from L. salvarius and L. sakei provided the highest binding response and interacted with κ-casein at all the tested pH values, i.e. in the range 4.0−5.5, and with β-casein at pH 4.0−5.0. When examined at pH 4.0, only HoPS from L. salvarius and L. sakei interacted with β-lactoglobulin. Under the tested conditions, HoPS from L. plantarum showed always either a lower binding response or no binding at all compared with HoPS from L. salvarius and L. sakei.","publication_date":{"day":null,"month":null,"year":2011,"errors":{}}},"translated_abstract":"Surface plasmon resonance-based biosensors enable the interaction between biomolecules to be monitored in real time with a label-free assay format. In the present study, the technique was used to assess the interaction between exopolysaccharides (EPS) and different milk proteins. The EPS were derived from three homopolysaccharide (HoPS)-producing Lactobacilli strains; Lactobacillus sakei, Lactobacillus plantarum, and Lactobacillus salvarius. The purified milk proteins applied were β-casein, β-lactoglobulin, and κ-casein. The results show that the binding capacity depends on the pH and decreases with increasing pH. HoPS from L. salvarius and L. sakei provided the highest binding response and interacted with κ-casein at all the tested pH values, i.e. in the range 4.0−5.5, and with β-casein at pH 4.0−5.0. When examined at pH 4.0, only HoPS from L. salvarius and L. sakei interacted with β-lactoglobulin. Under the tested conditions, HoPS from L. plantarum showed always either a lower binding response or no binding at all compared with HoPS from L. salvarius and L. sakei.","internal_url":"https://www.academia.edu/18184790/Using_Surface_Plasmon_Resonance_Technology_to_Screen_Interactions_Between_Exopolysaccharides_and_Milk_Proteins","translated_internal_url":"","created_at":"2015-11-12T00:16:17.563-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Using_Surface_Plasmon_Resonance_Technology_to_Screen_Interactions_Between_Exopolysaccharides_and_Milk_Proteins","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":229390,"name":"Real Time","url":"https://www.academia.edu/Documents/in/Real_Time"},{"id":1251963,"name":"Surface Plasmon","url":"https://www.academia.edu/Documents/in/Surface_Plasmon"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184788"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184788/Investigation_of_Consecutive_Fouling_and_Cleaning_Cycles_of_Ultrafiltration_Membranes_Used_for_Whey_Processing"><img alt="Research paper thumbnail of Investigation of Consecutive Fouling and Cleaning Cycles of Ultrafiltration Membranes Used for Whey Processing" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184788/Investigation_of_Consecutive_Fouling_and_Cleaning_Cycles_of_Ultrafiltration_Membranes_Used_for_Whey_Processing">Investigation of Consecutive Fouling and Cleaning Cycles of Ultrafiltration Membranes Used for Whey Processing</a></div><div class="wp-workCard_item"><span>International Journal of Food Engineering</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT Abstract: Development of resistance during multiple foulings and three-step Cleaning-In-...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">ABSTRACT Abstract: Development of resistance during multiple foulings and three-step Cleaning-In-Place (CIP) operations, simulating an industrial cleaning regime of polysulfone ultrafiltration membranes, was investigated. The study explored how trans-membrane pressure (150 and 300 kPa) and feed protein concentration (0.9 and 10%) influenced resistance reduction during filtration and flux recovery by the cleaning procedures. New membranes, pre-cleaned with a full CIP cycle, were used for each experiment. Subsequent fouling (simulating production) and CIP were done three times in a row and the development of fouling layer resistance was monitored and evaluated. Results show that filtration performance decreased during the first days of usage, possibly related to build-up of internal fouling. Cleaning success based on flux recovery was negatively influenced by a high protein concentration in the feed, but independent of the ransmembrane pressure during filtration.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184788"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184788"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184788; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184788]").text(description); $(".js-view-count[data-work-id=18184788]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184788; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184788']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184788, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184788]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184788,"title":"Investigation of Consecutive Fouling and Cleaning Cycles of Ultrafiltration Membranes Used for Whey Processing","translated_title":"","metadata":{"abstract":"ABSTRACT Abstract: Development of resistance during multiple foulings and three-step Cleaning-In-Place (CIP) operations, simulating an industrial cleaning regime of polysulfone ultrafiltration membranes, was investigated. The study explored how trans-membrane pressure (150 and 300 kPa) and feed protein concentration (0.9 and 10%) influenced resistance reduction during filtration and flux recovery by the cleaning procedures. New membranes, pre-cleaned with a full CIP cycle, were used for each experiment. Subsequent fouling (simulating production) and CIP were done three times in a row and the development of fouling layer resistance was monitored and evaluated. Results show that filtration performance decreased during the first days of usage, possibly related to build-up of internal fouling. 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Results show that filtration performance decreased during the first days of usage, possibly related to build-up of internal fouling. Cleaning success based on flux recovery was negatively influenced by a high protein concentration in the feed, but independent of the ransmembrane pressure during filtration.","internal_url":"https://www.academia.edu/18184788/Investigation_of_Consecutive_Fouling_and_Cleaning_Cycles_of_Ultrafiltration_Membranes_Used_for_Whey_Processing","translated_internal_url":"","created_at":"2015-11-12T00:16:17.466-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Investigation_of_Consecutive_Fouling_and_Cleaning_Cycles_of_Ultrafiltration_Membranes_Used_for_Whey_Processing","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":4468,"name":"Food Engineering","url":"https://www.academia.edu/Documents/in/Food_Engineering"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184786"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184786/Stability_of_cheese_emulsions_for_spray_drying"><img alt="Research paper thumbnail of Stability of cheese emulsions for spray drying" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184786/Stability_of_cheese_emulsions_for_spray_drying">Stability of cheese emulsions for spray drying</a></div><div class="wp-workCard_item"><span>International Dairy Journal</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT In cheese powder production, cheese is melted with water and emulsifying salt to create ...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">ABSTRACT In cheese powder production, cheese is melted with water and emulsifying salt to create an emulsion (denoted cheese feed) that should remain stable until and during spray drying. The aim of this study was to investigate how reduction of emulsifying salt may be compensated for by use of different combinations of cheese types. Cheese feeds were produced at laboratory scale from combinations of Cheddar, Camembert and soft white cheese. Methods for feed characterisation and determination of phase separation of feed were evaluated for applicability to describe the characteristics of the cheese feed. Cheese feed stability generally decreased when the concentration of emulsifying salt was reduced. Emulsion stability of cheese feeds of Cheddar in combination with either soft white cheese or, especially, Camembert were generally higher than for feeds produced with Cheddar only. The functionalities of stabilisation may be related to pH, calcium concentration, level of intact casein and salt-to-moisture ratio.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184786"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184786"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184786; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184786]").text(description); $(".js-view-count[data-work-id=18184786]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184786; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184786']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184786, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184786]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184786,"title":"Stability of cheese emulsions for spray drying","translated_title":"","metadata":{"abstract":"ABSTRACT In cheese powder production, cheese is melted with water and emulsifying salt to create an emulsion (denoted cheese feed) that should remain stable until and during spray drying. The aim of this study was to investigate how reduction of emulsifying salt may be compensated for by use of different combinations of cheese types. Cheese feeds were produced at laboratory scale from combinations of Cheddar, Camembert and soft white cheese. Methods for feed characterisation and determination of phase separation of feed were evaluated for applicability to describe the characteristics of the cheese feed. Cheese feed stability generally decreased when the concentration of emulsifying salt was reduced. Emulsion stability of cheese feeds of Cheddar in combination with either soft white cheese or, especially, Camembert were generally higher than for feeds produced with Cheddar only. The functionalities of stabilisation may be related to pH, calcium concentration, level of intact casein and salt-to-moisture ratio.","publication_date":{"day":null,"month":null,"year":2014,"errors":{}},"publication_name":"International Dairy Journal"},"translated_abstract":"ABSTRACT In cheese powder production, cheese is melted with water and emulsifying salt to create an emulsion (denoted cheese feed) that should remain stable until and during spray drying. The aim of this study was to investigate how reduction of emulsifying salt may be compensated for by use of different combinations of cheese types. Cheese feeds were produced at laboratory scale from combinations of Cheddar, Camembert and soft white cheese. Methods for feed characterisation and determination of phase separation of feed were evaluated for applicability to describe the characteristics of the cheese feed. Cheese feed stability generally decreased when the concentration of emulsifying salt was reduced. Emulsion stability of cheese feeds of Cheddar in combination with either soft white cheese or, especially, Camembert were generally higher than for feeds produced with Cheddar only. The functionalities of stabilisation may be related to pH, calcium concentration, level of intact casein and salt-to-moisture ratio.","internal_url":"https://www.academia.edu/18184786/Stability_of_cheese_emulsions_for_spray_drying","translated_internal_url":"","created_at":"2015-11-12T00:16:17.341-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Stability_of_cheese_emulsions_for_spray_drying","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":181926,"name":"Dairy","url":"https://www.academia.edu/Documents/in/Dairy"},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184784"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184784/Effect_of_partial_hydrolysis_with_an_immobilized_proteinase_on_thermal_gelation_properties_of_%CE%B2_lactoglobulin_B"><img alt="Research paper thumbnail of Effect of partial hydrolysis with an immobilized proteinase on thermal gelation properties of β-lactoglobulin B" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184784/Effect_of_partial_hydrolysis_with_an_immobilized_proteinase_on_thermal_gelation_properties_of_%CE%B2_lactoglobulin_B">Effect of partial hydrolysis with an immobilized proteinase on thermal gelation properties of β-lactoglobulin B</a></div><div class="wp-workCard_item"><span>Journal of Dairy Research</span><span>, 2000</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">We have investigated the influence of partial hydrolysis with an immobilized proteinase from Baci...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">We have investigated the influence of partial hydrolysis with an immobilized proteinase from Bacillus licheniformis on the thermal gelation of isolated beta-lactoglobulin B. Gelation behaviour was determined by dynamic rheological measurements (small deformation) and the gels were characterized with respect to microstructure and water-holding properties. A fine-stranded gel with a complex modulus of approximately 2000 Pa was formed from beta-lactoglobulin (50 g/l in 75 mM-Tris-HCl, pH 7.5). Limited hydrolysis prior to thermal gelation resulted in coarser gels with thicker protein strands and larger pores. Gel structure correlated with its permeability, proton mobility and water-holding capacity. Total stiffness gel increased with low degrees of hydrolysis, but decreased after prolonged hydrolysis. Maximal gel stiffness was 1.5-fold that gels made from of unhydrolysed beta-lactoglobulin. This was much lower than the stiffening effect obtained after partial hydrolysis of whey protein isolate, showing that the gel strengthening effect of partial hydrolysis was depedent on the protein composition and/or the hydrolysis and gelatin conditions. A mechanism to explain the observed effects of hydrolysis on gelation and gel properties is presented.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184784"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184784"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184784; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184784]").text(description); $(".js-view-count[data-work-id=18184784]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184784; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184784']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184784, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184784]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184784,"title":"Effect of partial hydrolysis with an immobilized proteinase on thermal gelation properties of β-lactoglobulin B","translated_title":"","metadata":{"abstract":"We have investigated the influence of partial hydrolysis with an immobilized proteinase from Bacillus licheniformis on the thermal gelation of isolated beta-lactoglobulin B. Gelation behaviour was determined by dynamic rheological measurements (small deformation) and the gels were characterized with respect to microstructure and water-holding properties. A fine-stranded gel with a complex modulus of approximately 2000 Pa was formed from beta-lactoglobulin (50 g/l in 75 mM-Tris-HCl, pH 7.5). Limited hydrolysis prior to thermal gelation resulted in coarser gels with thicker protein strands and larger pores. Gel structure correlated with its permeability, proton mobility and water-holding capacity. Total stiffness gel increased with low degrees of hydrolysis, but decreased after prolonged hydrolysis. Maximal gel stiffness was 1.5-fold that gels made from of unhydrolysed beta-lactoglobulin. This was much lower than the stiffening effect obtained after partial hydrolysis of whey protein isolate, showing that the gel strengthening effect of partial hydrolysis was depedent on the protein composition and/or the hydrolysis and gelatin conditions. A mechanism to explain the observed effects of hydrolysis on gelation and gel properties is presented.","publication_date":{"day":null,"month":null,"year":2000,"errors":{}},"publication_name":"Journal of Dairy Research"},"translated_abstract":"We have investigated the influence of partial hydrolysis with an immobilized proteinase from Bacillus licheniformis on the thermal gelation of isolated beta-lactoglobulin B. Gelation behaviour was determined by dynamic rheological measurements (small deformation) and the gels were characterized with respect to microstructure and water-holding properties. A fine-stranded gel with a complex modulus of approximately 2000 Pa was formed from beta-lactoglobulin (50 g/l in 75 mM-Tris-HCl, pH 7.5). Limited hydrolysis prior to thermal gelation resulted in coarser gels with thicker protein strands and larger pores. Gel structure correlated with its permeability, proton mobility and water-holding capacity. Total stiffness gel increased with low degrees of hydrolysis, but decreased after prolonged hydrolysis. Maximal gel stiffness was 1.5-fold that gels made from of unhydrolysed beta-lactoglobulin. This was much lower than the stiffening effect obtained after partial hydrolysis of whey protein isolate, showing that the gel strengthening effect of partial hydrolysis was depedent on the protein composition and/or the hydrolysis and gelatin conditions. A mechanism to explain the observed effects of hydrolysis on gelation and gel properties is presented.","internal_url":"https://www.academia.edu/18184784/Effect_of_partial_hydrolysis_with_an_immobilized_proteinase_on_thermal_gelation_properties_of_%CE%B2_lactoglobulin_B","translated_internal_url":"","created_at":"2015-11-12T00:16:17.236-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Effect_of_partial_hydrolysis_with_an_immobilized_proteinase_on_thermal_gelation_properties_of_β_lactoglobulin_B","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics"},{"id":7598,"name":"Rheology","url":"https://www.academia.edu/Documents/in/Rheology"},{"id":21732,"name":"Magnetic Resonance Spectroscopy","url":"https://www.academia.edu/Documents/in/Magnetic_Resonance_Spectroscopy"},{"id":29980,"name":"Animal Production","url":"https://www.academia.edu/Documents/in/Animal_Production"},{"id":83972,"name":"Permeability","url":"https://www.academia.edu/Documents/in/Permeability"},{"id":109384,"name":"Viscosity","url":"https://www.academia.edu/Documents/in/Viscosity"},{"id":112332,"name":"Bacillus","url":"https://www.academia.edu/Documents/in/Bacillus"},{"id":181926,"name":"Dairy","url":"https://www.academia.edu/Documents/in/Dairy"},{"id":246560,"name":"High Pressure Liquid Chromatography","url":"https://www.academia.edu/Documents/in/High_Pressure_Liquid_Chromatography"},{"id":284907,"name":"Gels","url":"https://www.academia.edu/Documents/in/Gels"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"},{"id":1030794,"name":"Hydrolysis","url":"https://www.academia.edu/Documents/in/Hydrolysis"},{"id":1491514,"name":"*Hot Temperature","url":"https://www.academia.edu/Documents/in/_Hot_Temperature"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> </div><div class="profile--tab_content_container js-tab-pane tab-pane" data-section-id="3392894" id="papers"><div class="js-work-strip profile--work_container" data-work-id="18184832"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184832/Stabilization_of_acidified_milk_drinks_using_pectin"><img alt="Research paper thumbnail of Stabilization of acidified milk drinks using pectin" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184832/Stabilization_of_acidified_milk_drinks_using_pectin">Stabilization of acidified milk drinks using pectin</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The present study was carried out based on a special capacity of high methoxyl pectin in stabiliz...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The present study was carried out based on a special capacity of high methoxyl pectin in stabilizing acidified milk drinks. The presence of an optimal concentration of high methoxyl pectin can prevent the defects of acidified milk drinks such as protein flocculation, sedimentation and macroscopic wheying-off. A narrow range of pectin including 0, 0.1, 0.15, 0.2, 0.25, 0.3, and 0.4%</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184832"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184832"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184832; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184832]").text(description); $(".js-view-count[data-work-id=18184832]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184832; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184832']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184832, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184832]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184832,"title":"Stabilization of acidified milk drinks using pectin","translated_title":"","metadata":{"abstract":"The present study was carried out based on a special capacity of high methoxyl pectin in stabilizing acidified milk drinks. 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A narrow range of pectin including 0, 0.1, 0.15, 0.2, 0.25, 0.3, and 0.4%","internal_url":"https://www.academia.edu/18184832/Stabilization_of_acidified_milk_drinks_using_pectin","translated_internal_url":"","created_at":"2015-11-12T00:16:20.495-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Stabilization_of_acidified_milk_drinks_using_pectin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":390245,"name":"Particle Size","url":"https://www.academia.edu/Documents/in/Particle_Size"}],"urls":[{"id":6034496,"url":"http://www.ajofai.info/abstract/stabilization%20of%20acidified%20milk%20drinks%20using%20pectin.pdf"}]}, dispatcherData: dispatcherData }); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184797"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184797/Effect_of_high_pressure_on_aggregation_and_thermal_gelation_of_%CE%B2_lactoglobulin"><img alt="Research paper thumbnail of Effect of high pressure on aggregation and thermal gelation of β-lactoglobulin" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184797/Effect_of_high_pressure_on_aggregation_and_thermal_gelation_of_%CE%B2_lactoglobulin">Effect of high pressure on aggregation and thermal gelation of β-lactoglobulin</a></div><div class="wp-workCard_item"><span>Milchwissenschaft</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Solutions containing 5% purified β-Lg B at pH 7.5 were subjected to high pressure treatments of v...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Solutions containing 5% purified β-Lg B at pH 7.5 were subjected to high pressure treatments of varying intensity and duration. The state of aggregation and the thermal gelation properties of the pressure-treated samples were monitored immediately after depressurization and after storage for 24 h at 5°C. A pressure of 150 MPa applied for 30 min or pressures in excess of 300 MPa applied for 0 or 30 min led to formation of soluble aggregates. When continued for 30 min, a pressure of 450 MPa caused gelation of the 5% β-Lg solution. The state of aggregation of the protein changed over time, generally with an increasing proportion of polymers. For samples measured after 24 h of storage a good inverse correlation was found between pressure intensity, proportion of polymers and thermal gelation properties. With increasing pressure, the time of gelation increased and the total gel stiffness decreased.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184797"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184797"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184797; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184797]").text(description); $(".js-view-count[data-work-id=18184797]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184797; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184797']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184797, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184797]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184797,"title":"Effect of high pressure on aggregation and thermal gelation of β-lactoglobulin","translated_title":"","metadata":{"abstract":"Solutions containing 5% purified β-Lg B at pH 7.5 were subjected to high pressure treatments of varying intensity and duration. The state of aggregation and the thermal gelation properties of the pressure-treated samples were monitored immediately after depressurization and after storage for 24 h at 5°C. A pressure of 150 MPa applied for 30 min or pressures in excess of 300 MPa applied for 0 or 30 min led to formation of soluble aggregates. When continued for 30 min, a pressure of 450 MPa caused gelation of the 5% β-Lg solution. The state of aggregation of the protein changed over time, generally with an increasing proportion of polymers. For samples measured after 24 h of storage a good inverse correlation was found between pressure intensity, proportion of polymers and thermal gelation properties. With increasing pressure, the time of gelation increased and the total gel stiffness decreased.","publication_name":"Milchwissenschaft"},"translated_abstract":"Solutions containing 5% purified β-Lg B at pH 7.5 were subjected to high pressure treatments of varying intensity and duration. The state of aggregation and the thermal gelation properties of the pressure-treated samples were monitored immediately after depressurization and after storage for 24 h at 5°C. A pressure of 150 MPa applied for 30 min or pressures in excess of 300 MPa applied for 0 or 30 min led to formation of soluble aggregates. When continued for 30 min, a pressure of 450 MPa caused gelation of the 5% β-Lg solution. The state of aggregation of the protein changed over time, generally with an increasing proportion of polymers. For samples measured after 24 h of storage a good inverse correlation was found between pressure intensity, proportion of polymers and thermal gelation properties. With increasing pressure, the time of gelation increased and the total gel stiffness decreased.","internal_url":"https://www.academia.edu/18184797/Effect_of_high_pressure_on_aggregation_and_thermal_gelation_of_%CE%B2_lactoglobulin","translated_internal_url":"","created_at":"2015-11-12T00:16:18.026-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Effect_of_high_pressure_on_aggregation_and_thermal_gelation_of_β_lactoglobulin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184795"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184795/Formation_of_nanotubes_and_gels_at_a_broad_pH_range_upon_partial_hydrolysis_of_bovine_%CE%B1_lactalbumin"><img alt="Research paper thumbnail of Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184795/Formation_of_nanotubes_and_gels_at_a_broad_pH_range_upon_partial_hydrolysis_of_bovine_%CE%B1_lactalbumin">Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin</a></div><div class="wp-workCard_item"><span>International Dairy Journal</span><span>, 2015</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184795"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184795"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184795; 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dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184795]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184795,"title":"Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin","translated_title":"","metadata":{"publication_date":{"day":null,"month":null,"year":2015,"errors":{}},"publication_name":"International Dairy Journal"},"translated_abstract":null,"internal_url":"https://www.academia.edu/18184795/Formation_of_nanotubes_and_gels_at_a_broad_pH_range_upon_partial_hydrolysis_of_bovine_%CE%B1_lactalbumin","translated_internal_url":"","created_at":"2015-11-12T00:16:17.902-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Formation_of_nanotubes_and_gels_at_a_broad_pH_range_upon_partial_hydrolysis_of_bovine_α_lactalbumin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":181926,"name":"Dairy","url":"https://www.academia.edu/Documents/in/Dairy"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184793"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184793/Pilot_scale_purification_of_%CE%B1_lactalbumin_from_enriched_whey_protein_concentrate_by_anion_exchange_chromatography_and_ultrafiltration"><img alt="Research paper thumbnail of Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184793/Pilot_scale_purification_of_%CE%B1_lactalbumin_from_enriched_whey_protein_concentrate_by_anion_exchange_chromatography_and_ultrafiltration">Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration</a></div><div class="wp-workCard_item"><span>Dairy Science & Technology</span><span>, 2015</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT A method based on anion exchange chromatography (AIEX) in combination with ultrafiltrati...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">ABSTRACT A method based on anion exchange chromatography (AIEX) in combination with ultrafiltration (UF) was developed to obtain kilogram-scale amounts of bovine α-lactalbumin (α-La) of high purity from α-La-enriched whey protein concentrate (αWPC). Initially, α-La was successfully purified, at laboratory scale, from a 10% solution of αWPC. Removal of casein and denatured whey protein by acid precipitation resulted in a α-La purity of 78%. A further purification by AIEX eluting with sodium acetate (NaAc) buffer led to a final purity and recovery of 100 and 85%, respectively. Based on this, the process was simplified and optimized for pilot-scale purification by selective binding of β-lactoglobulin (β-Lg). Batchwise expanded bed AIEX using a column with 5 L of Q Sepharose matrix was performed. Pure α-La was obtained in the run through buffer. In the end, 1100 g of holo form α-La was obtained with a purity of 97.4% in protein and a recovery of 80%, calculated based on the protein detectable in reversed phase high-performance liquid chromatography (RP-HPLC). Thus, by combining AIEX and UF, heating was avoided allowing production of α-La in kilo-scale with high purity and recovery from αWPC with a minimum volume of buffer solutions.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184793"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184793"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184793; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184793]").text(description); $(".js-view-count[data-work-id=18184793]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184793; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184793']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184793, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184793]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184793,"title":"Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration","translated_title":"","metadata":{"abstract":"ABSTRACT A method based on anion exchange chromatography (AIEX) in combination with ultrafiltration (UF) was developed to obtain kilogram-scale amounts of bovine α-lactalbumin (α-La) of high purity from α-La-enriched whey protein concentrate (αWPC). Initially, α-La was successfully purified, at laboratory scale, from a 10% solution of αWPC. Removal of casein and denatured whey protein by acid precipitation resulted in a α-La purity of 78%. A further purification by AIEX eluting with sodium acetate (NaAc) buffer led to a final purity and recovery of 100 and 85%, respectively. Based on this, the process was simplified and optimized for pilot-scale purification by selective binding of β-lactoglobulin (β-Lg). Batchwise expanded bed AIEX using a column with 5 L of Q Sepharose matrix was performed. Pure α-La was obtained in the run through buffer. In the end, 1100 g of holo form α-La was obtained with a purity of 97.4% in protein and a recovery of 80%, calculated based on the protein detectable in reversed phase high-performance liquid chromatography (RP-HPLC). Thus, by combining AIEX and UF, heating was avoided allowing production of α-La in kilo-scale with high purity and recovery from αWPC with a minimum volume of buffer solutions.","publication_date":{"day":null,"month":null,"year":2015,"errors":{}},"publication_name":"Dairy Science \u0026 Technology"},"translated_abstract":"ABSTRACT A method based on anion exchange chromatography (AIEX) in combination with ultrafiltration (UF) was developed to obtain kilogram-scale amounts of bovine α-lactalbumin (α-La) of high purity from α-La-enriched whey protein concentrate (αWPC). Initially, α-La was successfully purified, at laboratory scale, from a 10% solution of αWPC. Removal of casein and denatured whey protein by acid precipitation resulted in a α-La purity of 78%. A further purification by AIEX eluting with sodium acetate (NaAc) buffer led to a final purity and recovery of 100 and 85%, respectively. Based on this, the process was simplified and optimized for pilot-scale purification by selective binding of β-lactoglobulin (β-Lg). Batchwise expanded bed AIEX using a column with 5 L of Q Sepharose matrix was performed. Pure α-La was obtained in the run through buffer. In the end, 1100 g of holo form α-La was obtained with a purity of 97.4% in protein and a recovery of 80%, calculated based on the protein detectable in reversed phase high-performance liquid chromatography (RP-HPLC). Thus, by combining AIEX and UF, heating was avoided allowing production of α-La in kilo-scale with high purity and recovery from αWPC with a minimum volume of buffer solutions.","internal_url":"https://www.academia.edu/18184793/Pilot_scale_purification_of_%CE%B1_lactalbumin_from_enriched_whey_protein_concentrate_by_anion_exchange_chromatography_and_ultrafiltration","translated_internal_url":"","created_at":"2015-11-12T00:16:17.789-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Pilot_scale_purification_of_α_lactalbumin_from_enriched_whey_protein_concentrate_by_anion_exchange_chromatography_and_ultrafiltration","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":60,"name":"Mechanical Engineering","url":"https://www.academia.edu/Documents/in/Mechanical_Engineering"},{"id":42955,"name":"Dairy Science and Technology","url":"https://www.academia.edu/Documents/in/Dairy_Science_and_Technology"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184791"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184791/Emulsifying_salt_increase_stability_of_cheese_emulsions_during_holding"><img alt="Research paper thumbnail of Emulsifying salt increase stability of cheese emulsions during holding" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184791/Emulsifying_salt_increase_stability_of_cheese_emulsions_during_holding">Emulsifying salt increase stability of cheese emulsions during holding</a></div><div class="wp-workCard_item"><span>LWT - Food Science and Technology</span><span>, 2015</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT In cheese powder production, cheese is mixed and melted with water and emulsifying salt ...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">ABSTRACT In cheese powder production, cheese is mixed and melted with water and emulsifying salt to form an emulsion (cheese feed) which is required to remain stable at 60 °C for 1 h and during further processing until spray drying. Addition of emulsifying salts ensures this, but recent demands for reduction of sodium and phosphate in foods makes production of cheese powder without or with minimal amounts of emulsifying salts desirable. The present work uses a centrifugation method to characterize stability of model cheese feeds. Stability of cheese feed with emulsifying salt increased with holding time at 60 °C, especially when no stirring was applied. No change in stability during holding was observed in cheese feeds without emulsifying salt. This effect is suggested to be due to continued exerted functionality of the emulsifying salt, possibly through reorganizations of the mineral balance.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184791"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184791"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184791; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184791]").text(description); $(".js-view-count[data-work-id=18184791]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184791; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184791']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184791, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184791]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184791,"title":"Emulsifying salt increase stability of cheese emulsions during holding","translated_title":"","metadata":{"abstract":"ABSTRACT In cheese powder production, cheese is mixed and melted with water and emulsifying salt to form an emulsion (cheese feed) which is required to remain stable at 60 °C for 1 h and during further processing until spray drying. Addition of emulsifying salts ensures this, but recent demands for reduction of sodium and phosphate in foods makes production of cheese powder without or with minimal amounts of emulsifying salts desirable. The present work uses a centrifugation method to characterize stability of model cheese feeds. Stability of cheese feed with emulsifying salt increased with holding time at 60 °C, especially when no stirring was applied. No change in stability during holding was observed in cheese feeds without emulsifying salt. This effect is suggested to be due to continued exerted functionality of the emulsifying salt, possibly through reorganizations of the mineral balance.","publication_date":{"day":null,"month":null,"year":2015,"errors":{}},"publication_name":"LWT - Food Science and Technology"},"translated_abstract":"ABSTRACT In cheese powder production, cheese is mixed and melted with water and emulsifying salt to form an emulsion (cheese feed) which is required to remain stable at 60 °C for 1 h and during further processing until spray drying. Addition of emulsifying salts ensures this, but recent demands for reduction of sodium and phosphate in foods makes production of cheese powder without or with minimal amounts of emulsifying salts desirable. The present work uses a centrifugation method to characterize stability of model cheese feeds. Stability of cheese feed with emulsifying salt increased with holding time at 60 °C, especially when no stirring was applied. No change in stability during holding was observed in cheese feeds without emulsifying salt. This effect is suggested to be due to continued exerted functionality of the emulsifying salt, possibly through reorganizations of the mineral balance.","internal_url":"https://www.academia.edu/18184791/Emulsifying_salt_increase_stability_of_cheese_emulsions_during_holding","translated_internal_url":"","created_at":"2015-11-12T00:16:17.663-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Emulsifying_salt_increase_stability_of_cheese_emulsions_during_holding","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":29980,"name":"Animal Production","url":"https://www.academia.edu/Documents/in/Animal_Production"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184790"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184790/Using_Surface_Plasmon_Resonance_Technology_to_Screen_Interactions_Between_Exopolysaccharides_and_Milk_Proteins"><img alt="Research paper thumbnail of Using Surface Plasmon Resonance Technology to Screen Interactions Between Exopolysaccharides and Milk Proteins" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184790/Using_Surface_Plasmon_Resonance_Technology_to_Screen_Interactions_Between_Exopolysaccharides_and_Milk_Proteins">Using Surface Plasmon Resonance Technology to Screen Interactions Between Exopolysaccharides and Milk Proteins</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Surface plasmon resonance-based biosensors enable the interaction between biomolecules to be moni...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Surface plasmon resonance-based biosensors enable the interaction between biomolecules to be monitored in real time with a label-free assay format. In the present study, the technique was used to assess the interaction between exopolysaccharides (EPS) and different milk proteins. The EPS were derived from three homopolysaccharide (HoPS)-producing Lactobacilli strains; Lactobacillus sakei, Lactobacillus plantarum, and Lactobacillus salvarius. The purified milk proteins applied were β-casein, β-lactoglobulin, and κ-casein. The results show that the binding capacity depends on the pH and decreases with increasing pH. HoPS from L. salvarius and L. sakei provided the highest binding response and interacted with κ-casein at all the tested pH values, i.e. in the range 4.0−5.5, and with β-casein at pH 4.0−5.0. When examined at pH 4.0, only HoPS from L. salvarius and L. sakei interacted with β-lactoglobulin. Under the tested conditions, HoPS from L. plantarum showed always either a lower binding response or no binding at all compared with HoPS from L. salvarius and L. sakei.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184790"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184790"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184790; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184790]").text(description); $(".js-view-count[data-work-id=18184790]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184790; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184790']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184790, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184790]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184790,"title":"Using Surface Plasmon Resonance Technology to Screen Interactions Between Exopolysaccharides and Milk Proteins","translated_title":"","metadata":{"abstract":"Surface plasmon resonance-based biosensors enable the interaction between biomolecules to be monitored in real time with a label-free assay format. In the present study, the technique was used to assess the interaction between exopolysaccharides (EPS) and different milk proteins. The EPS were derived from three homopolysaccharide (HoPS)-producing Lactobacilli strains; Lactobacillus sakei, Lactobacillus plantarum, and Lactobacillus salvarius. The purified milk proteins applied were β-casein, β-lactoglobulin, and κ-casein. The results show that the binding capacity depends on the pH and decreases with increasing pH. HoPS from L. salvarius and L. sakei provided the highest binding response and interacted with κ-casein at all the tested pH values, i.e. in the range 4.0−5.5, and with β-casein at pH 4.0−5.0. When examined at pH 4.0, only HoPS from L. salvarius and L. sakei interacted with β-lactoglobulin. Under the tested conditions, HoPS from L. plantarum showed always either a lower binding response or no binding at all compared with HoPS from L. salvarius and L. sakei.","publication_date":{"day":null,"month":null,"year":2011,"errors":{}}},"translated_abstract":"Surface plasmon resonance-based biosensors enable the interaction between biomolecules to be monitored in real time with a label-free assay format. In the present study, the technique was used to assess the interaction between exopolysaccharides (EPS) and different milk proteins. The EPS were derived from three homopolysaccharide (HoPS)-producing Lactobacilli strains; Lactobacillus sakei, Lactobacillus plantarum, and Lactobacillus salvarius. The purified milk proteins applied were β-casein, β-lactoglobulin, and κ-casein. The results show that the binding capacity depends on the pH and decreases with increasing pH. HoPS from L. salvarius and L. sakei provided the highest binding response and interacted with κ-casein at all the tested pH values, i.e. in the range 4.0−5.5, and with β-casein at pH 4.0−5.0. When examined at pH 4.0, only HoPS from L. salvarius and L. sakei interacted with β-lactoglobulin. Under the tested conditions, HoPS from L. plantarum showed always either a lower binding response or no binding at all compared with HoPS from L. salvarius and L. sakei.","internal_url":"https://www.academia.edu/18184790/Using_Surface_Plasmon_Resonance_Technology_to_Screen_Interactions_Between_Exopolysaccharides_and_Milk_Proteins","translated_internal_url":"","created_at":"2015-11-12T00:16:17.563-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Using_Surface_Plasmon_Resonance_Technology_to_Screen_Interactions_Between_Exopolysaccharides_and_Milk_Proteins","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":229390,"name":"Real Time","url":"https://www.academia.edu/Documents/in/Real_Time"},{"id":1251963,"name":"Surface Plasmon","url":"https://www.academia.edu/Documents/in/Surface_Plasmon"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184788"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184788/Investigation_of_Consecutive_Fouling_and_Cleaning_Cycles_of_Ultrafiltration_Membranes_Used_for_Whey_Processing"><img alt="Research paper thumbnail of Investigation of Consecutive Fouling and Cleaning Cycles of Ultrafiltration Membranes Used for Whey Processing" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184788/Investigation_of_Consecutive_Fouling_and_Cleaning_Cycles_of_Ultrafiltration_Membranes_Used_for_Whey_Processing">Investigation of Consecutive Fouling and Cleaning Cycles of Ultrafiltration Membranes Used for Whey Processing</a></div><div class="wp-workCard_item"><span>International Journal of Food Engineering</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT Abstract: Development of resistance during multiple foulings and three-step Cleaning-In-...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">ABSTRACT Abstract: Development of resistance during multiple foulings and three-step Cleaning-In-Place (CIP) operations, simulating an industrial cleaning regime of polysulfone ultrafiltration membranes, was investigated. The study explored how trans-membrane pressure (150 and 300 kPa) and feed protein concentration (0.9 and 10%) influenced resistance reduction during filtration and flux recovery by the cleaning procedures. New membranes, pre-cleaned with a full CIP cycle, were used for each experiment. Subsequent fouling (simulating production) and CIP were done three times in a row and the development of fouling layer resistance was monitored and evaluated. Results show that filtration performance decreased during the first days of usage, possibly related to build-up of internal fouling. Cleaning success based on flux recovery was negatively influenced by a high protein concentration in the feed, but independent of the ransmembrane pressure during filtration.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184788"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184788"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184788; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184788]").text(description); $(".js-view-count[data-work-id=18184788]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184788; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184788']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184788, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184788]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184788,"title":"Investigation of Consecutive Fouling and Cleaning Cycles of Ultrafiltration Membranes Used for Whey Processing","translated_title":"","metadata":{"abstract":"ABSTRACT Abstract: Development of resistance during multiple foulings and three-step Cleaning-In-Place (CIP) operations, simulating an industrial cleaning regime of polysulfone ultrafiltration membranes, was investigated. The study explored how trans-membrane pressure (150 and 300 kPa) and feed protein concentration (0.9 and 10%) influenced resistance reduction during filtration and flux recovery by the cleaning procedures. New membranes, pre-cleaned with a full CIP cycle, were used for each experiment. Subsequent fouling (simulating production) and CIP were done three times in a row and the development of fouling layer resistance was monitored and evaluated. Results show that filtration performance decreased during the first days of usage, possibly related to build-up of internal fouling. 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Results show that filtration performance decreased during the first days of usage, possibly related to build-up of internal fouling. Cleaning success based on flux recovery was negatively influenced by a high protein concentration in the feed, but independent of the ransmembrane pressure during filtration.","internal_url":"https://www.academia.edu/18184788/Investigation_of_Consecutive_Fouling_and_Cleaning_Cycles_of_Ultrafiltration_Membranes_Used_for_Whey_Processing","translated_internal_url":"","created_at":"2015-11-12T00:16:17.466-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Investigation_of_Consecutive_Fouling_and_Cleaning_Cycles_of_Ultrafiltration_Membranes_Used_for_Whey_Processing","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":4468,"name":"Food Engineering","url":"https://www.academia.edu/Documents/in/Food_Engineering"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184786"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184786/Stability_of_cheese_emulsions_for_spray_drying"><img alt="Research paper thumbnail of Stability of cheese emulsions for spray drying" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184786/Stability_of_cheese_emulsions_for_spray_drying">Stability of cheese emulsions for spray drying</a></div><div class="wp-workCard_item"><span>International Dairy Journal</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT In cheese powder production, cheese is melted with water and emulsifying salt to create ...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">ABSTRACT In cheese powder production, cheese is melted with water and emulsifying salt to create an emulsion (denoted cheese feed) that should remain stable until and during spray drying. The aim of this study was to investigate how reduction of emulsifying salt may be compensated for by use of different combinations of cheese types. Cheese feeds were produced at laboratory scale from combinations of Cheddar, Camembert and soft white cheese. Methods for feed characterisation and determination of phase separation of feed were evaluated for applicability to describe the characteristics of the cheese feed. Cheese feed stability generally decreased when the concentration of emulsifying salt was reduced. Emulsion stability of cheese feeds of Cheddar in combination with either soft white cheese or, especially, Camembert were generally higher than for feeds produced with Cheddar only. The functionalities of stabilisation may be related to pH, calcium concentration, level of intact casein and salt-to-moisture ratio.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184786"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184786"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184786; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184786]").text(description); $(".js-view-count[data-work-id=18184786]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184786; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184786']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184786, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184786]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184786,"title":"Stability of cheese emulsions for spray drying","translated_title":"","metadata":{"abstract":"ABSTRACT In cheese powder production, cheese is melted with water and emulsifying salt to create an emulsion (denoted cheese feed) that should remain stable until and during spray drying. The aim of this study was to investigate how reduction of emulsifying salt may be compensated for by use of different combinations of cheese types. Cheese feeds were produced at laboratory scale from combinations of Cheddar, Camembert and soft white cheese. Methods for feed characterisation and determination of phase separation of feed were evaluated for applicability to describe the characteristics of the cheese feed. Cheese feed stability generally decreased when the concentration of emulsifying salt was reduced. Emulsion stability of cheese feeds of Cheddar in combination with either soft white cheese or, especially, Camembert were generally higher than for feeds produced with Cheddar only. The functionalities of stabilisation may be related to pH, calcium concentration, level of intact casein and salt-to-moisture ratio.","publication_date":{"day":null,"month":null,"year":2014,"errors":{}},"publication_name":"International Dairy Journal"},"translated_abstract":"ABSTRACT In cheese powder production, cheese is melted with water and emulsifying salt to create an emulsion (denoted cheese feed) that should remain stable until and during spray drying. The aim of this study was to investigate how reduction of emulsifying salt may be compensated for by use of different combinations of cheese types. Cheese feeds were produced at laboratory scale from combinations of Cheddar, Camembert and soft white cheese. Methods for feed characterisation and determination of phase separation of feed were evaluated for applicability to describe the characteristics of the cheese feed. Cheese feed stability generally decreased when the concentration of emulsifying salt was reduced. Emulsion stability of cheese feeds of Cheddar in combination with either soft white cheese or, especially, Camembert were generally higher than for feeds produced with Cheddar only. The functionalities of stabilisation may be related to pH, calcium concentration, level of intact casein and salt-to-moisture ratio.","internal_url":"https://www.academia.edu/18184786/Stability_of_cheese_emulsions_for_spray_drying","translated_internal_url":"","created_at":"2015-11-12T00:16:17.341-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Stability_of_cheese_emulsions_for_spray_drying","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":181926,"name":"Dairy","url":"https://www.academia.edu/Documents/in/Dairy"},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="18184784"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/18184784/Effect_of_partial_hydrolysis_with_an_immobilized_proteinase_on_thermal_gelation_properties_of_%CE%B2_lactoglobulin_B"><img alt="Research paper thumbnail of Effect of partial hydrolysis with an immobilized proteinase on thermal gelation properties of β-lactoglobulin B" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/18184784/Effect_of_partial_hydrolysis_with_an_immobilized_proteinase_on_thermal_gelation_properties_of_%CE%B2_lactoglobulin_B">Effect of partial hydrolysis with an immobilized proteinase on thermal gelation properties of β-lactoglobulin B</a></div><div class="wp-workCard_item"><span>Journal of Dairy Research</span><span>, 2000</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">We have investigated the influence of partial hydrolysis with an immobilized proteinase from Baci...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">We have investigated the influence of partial hydrolysis with an immobilized proteinase from Bacillus licheniformis on the thermal gelation of isolated beta-lactoglobulin B. Gelation behaviour was determined by dynamic rheological measurements (small deformation) and the gels were characterized with respect to microstructure and water-holding properties. A fine-stranded gel with a complex modulus of approximately 2000 Pa was formed from beta-lactoglobulin (50 g/l in 75 mM-Tris-HCl, pH 7.5). Limited hydrolysis prior to thermal gelation resulted in coarser gels with thicker protein strands and larger pores. Gel structure correlated with its permeability, proton mobility and water-holding capacity. Total stiffness gel increased with low degrees of hydrolysis, but decreased after prolonged hydrolysis. Maximal gel stiffness was 1.5-fold that gels made from of unhydrolysed beta-lactoglobulin. This was much lower than the stiffening effect obtained after partial hydrolysis of whey protein isolate, showing that the gel strengthening effect of partial hydrolysis was depedent on the protein composition and/or the hydrolysis and gelatin conditions. A mechanism to explain the observed effects of hydrolysis on gelation and gel properties is presented.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="18184784"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="18184784"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18184784; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18184784]").text(description); $(".js-view-count[data-work-id=18184784]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18184784; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='18184784']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 18184784, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=18184784]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":18184784,"title":"Effect of partial hydrolysis with an immobilized proteinase on thermal gelation properties of β-lactoglobulin B","translated_title":"","metadata":{"abstract":"We have investigated the influence of partial hydrolysis with an immobilized proteinase from Bacillus licheniformis on the thermal gelation of isolated beta-lactoglobulin B. Gelation behaviour was determined by dynamic rheological measurements (small deformation) and the gels were characterized with respect to microstructure and water-holding properties. A fine-stranded gel with a complex modulus of approximately 2000 Pa was formed from beta-lactoglobulin (50 g/l in 75 mM-Tris-HCl, pH 7.5). Limited hydrolysis prior to thermal gelation resulted in coarser gels with thicker protein strands and larger pores. Gel structure correlated with its permeability, proton mobility and water-holding capacity. Total stiffness gel increased with low degrees of hydrolysis, but decreased after prolonged hydrolysis. Maximal gel stiffness was 1.5-fold that gels made from of unhydrolysed beta-lactoglobulin. This was much lower than the stiffening effect obtained after partial hydrolysis of whey protein isolate, showing that the gel strengthening effect of partial hydrolysis was depedent on the protein composition and/or the hydrolysis and gelatin conditions. A mechanism to explain the observed effects of hydrolysis on gelation and gel properties is presented.","publication_date":{"day":null,"month":null,"year":2000,"errors":{}},"publication_name":"Journal of Dairy Research"},"translated_abstract":"We have investigated the influence of partial hydrolysis with an immobilized proteinase from Bacillus licheniformis on the thermal gelation of isolated beta-lactoglobulin B. Gelation behaviour was determined by dynamic rheological measurements (small deformation) and the gels were characterized with respect to microstructure and water-holding properties. A fine-stranded gel with a complex modulus of approximately 2000 Pa was formed from beta-lactoglobulin (50 g/l in 75 mM-Tris-HCl, pH 7.5). Limited hydrolysis prior to thermal gelation resulted in coarser gels with thicker protein strands and larger pores. Gel structure correlated with its permeability, proton mobility and water-holding capacity. Total stiffness gel increased with low degrees of hydrolysis, but decreased after prolonged hydrolysis. Maximal gel stiffness was 1.5-fold that gels made from of unhydrolysed beta-lactoglobulin. This was much lower than the stiffening effect obtained after partial hydrolysis of whey protein isolate, showing that the gel strengthening effect of partial hydrolysis was depedent on the protein composition and/or the hydrolysis and gelatin conditions. A mechanism to explain the observed effects of hydrolysis on gelation and gel properties is presented.","internal_url":"https://www.academia.edu/18184784/Effect_of_partial_hydrolysis_with_an_immobilized_proteinase_on_thermal_gelation_properties_of_%CE%B2_lactoglobulin_B","translated_internal_url":"","created_at":"2015-11-12T00:16:17.236-08:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33968931,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Effect_of_partial_hydrolysis_with_an_immobilized_proteinase_on_thermal_gelation_properties_of_β_lactoglobulin_B","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33968931,"first_name":"Richard","middle_initials":null,"last_name":"Ipsen","page_name":"RIpsen","domain_name":"ku-dk","created_at":"2015-08-17T00:30:31.444-07:00","display_name":"Richard Ipsen","url":"https://ku-dk.academia.edu/RIpsen"},"attachments":[],"research_interests":[{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics"},{"id":7598,"name":"Rheology","url":"https://www.academia.edu/Documents/in/Rheology"},{"id":21732,"name":"Magnetic Resonance Spectroscopy","url":"https://www.academia.edu/Documents/in/Magnetic_Resonance_Spectroscopy"},{"id":29980,"name":"Animal Production","url":"https://www.academia.edu/Documents/in/Animal_Production"},{"id":83972,"name":"Permeability","url":"https://www.academia.edu/Documents/in/Permeability"},{"id":109384,"name":"Viscosity","url":"https://www.academia.edu/Documents/in/Viscosity"},{"id":112332,"name":"Bacillus","url":"https://www.academia.edu/Documents/in/Bacillus"},{"id":181926,"name":"Dairy","url":"https://www.academia.edu/Documents/in/Dairy"},{"id":246560,"name":"High Pressure Liquid Chromatography","url":"https://www.academia.edu/Documents/in/High_Pressure_Liquid_Chromatography"},{"id":284907,"name":"Gels","url":"https://www.academia.edu/Documents/in/Gels"},{"id":573653,"name":"Food Sciences","url":"https://www.academia.edu/Documents/in/Food_Sciences"},{"id":1030794,"name":"Hydrolysis","url":"https://www.academia.edu/Documents/in/Hydrolysis"},{"id":1491514,"name":"*Hot Temperature","url":"https://www.academia.edu/Documents/in/_Hot_Temperature"}],"urls":[]}, dispatcherData: dispatcherData }); 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