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extraction</title> <meta name="description" content="Search results for: protein extraction"> <meta name="keywords" content="protein extraction"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar navbar-expand-lg navbar-light"> <a class="navbar-brand" href="https://waset.org"> <img src="https://cdn.waset.org/static/images/wasetc.png" alt="Open Science Research Excellence" title="Open Science Research Excellence" /> </a> <button class="d-block d-lg-none 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action="https://publications.waset.org/abstracts/search"> <div id="custom-search-input"> <div class="input-group"> <i class="fas fa-search"></i> <input type="text" class="search-query" name="q" placeholder="Author, Title, Abstract, Keywords" value="protein extraction"> <input type="submit" class="btn_search" value="Search"> </div> </div> </form> </div> </div> <div class="row mt-3"> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Commenced</strong> in January 2007</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Frequency:</strong> Monthly</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Edition:</strong> International</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Paper Count:</strong> 4237</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: protein extraction</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4237</span> Lentil Protein Fortification in Cranberry Squash</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sandhya%20Devi%20A">Sandhya Devi A</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The protein content of the cranberry squash (protein: 0g) may be increased by extracting protein from the lentils (9 g), which is particularly linked to a lower risk of developing heart disease. Using the technique of alkaline extraction from the lentils flour, protein may be extracted. Alkaline extraction of protein from lentil flour was optimized utilizing response surface approach in order to maximize both protein content and yield. Cranberry squash may be taken if a protein fortification syrup is prepared and processed into the squash. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alkaline%20extraction" title="alkaline extraction">alkaline extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=cranberry%20squash" title=" cranberry squash"> cranberry squash</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20fortification" title=" protein fortification"> protein fortification</a>, <a href="https://publications.waset.org/abstracts/search?q=response%20surface%20methodology" title=" response surface methodology"> response surface methodology</a> </p> <a href="https://publications.waset.org/abstracts/153178/lentil-protein-fortification-in-cranberry-squash" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/153178.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">111</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4236</span> Effect of Electromagnetic Fields on Protein Extraction from Shrimp By-Products for Electrospinning Process</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Guido%20Trautmann-S%C3%A1ez">Guido Trautmann-Sáez</a>, <a href="https://publications.waset.org/abstracts/search?q=Mario%20P%C3%A9rez-Won"> Mario Pérez-Won</a>, <a href="https://publications.waset.org/abstracts/search?q=Vilbett%20Briones"> Vilbett Briones</a>, <a href="https://publications.waset.org/abstracts/search?q=Mar%C3%ADa%20Jos%C3%A9%20Bugue%C3%B1o"> María José Bugueño</a>, <a href="https://publications.waset.org/abstracts/search?q=Gipsy%20Tabilo-Munizaga"> Gipsy Tabilo-Munizaga</a>, <a href="https://publications.waset.org/abstracts/search?q=Luis%20Gonz%C3%A1les-Cavieres"> Luis Gonzáles-Cavieres</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Shrimp by-products are a valuable source of protein. However, traditional protein extraction methods have limitations in terms of their efficiency. Protein extraction from shrimp (Pleuroncodes monodon) industrial by-products assisted with ohmic heating (OH), microwave (MW) and pulsed electric field (PEF). It was performed by chemical method (using NaOH and HCl 2M) assisted with OH, MW and PEF in a continuous flow system (5 ml/s). Protein determination, differential scanning calorimetry (DSC) and Fourier-transform infrared (FTIR). Results indicate a 19.25% (PEF) 3.65% (OH) and 28.19% (MW) improvement in protein extraction efficiency. The most efficient method was selected for the electrospinning process and obtaining fiber. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=electrospinning%20process" title="electrospinning process">electrospinning process</a>, <a href="https://publications.waset.org/abstracts/search?q=emerging%20technology" title=" emerging technology"> emerging technology</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20extraction" title=" protein extraction"> protein extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=shrimp%20by-products" title=" shrimp by-products"> shrimp by-products</a> </p> <a href="https://publications.waset.org/abstracts/171420/effect-of-electromagnetic-fields-on-protein-extraction-from-shrimp-by-products-for-electrospinning-process" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/171420.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">90</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4235</span> Protein and Lipid Extraction from Microalgae with Ultrasound Assisted Osmotic Shock Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Nais%20Pinta%20Adetya">Nais Pinta Adetya</a>, <a href="https://publications.waset.org/abstracts/search?q=H.%20Hadiyanto"> H. Hadiyanto</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Microalgae has a potential to be utilized as food and natural colorant. The microalgae components consists of three main parts, these are lipid, protein, and carbohydrate. Crucial step in producing lipid and protein from microalgae is extraction. Microalgae has high water level (70-90%), it causes drying process of biomass needs much more energy and also has potential to distract lipid and protein from microalgae. Extraction of lipid from wet biomass is able to take place efficiently with cell disruption of microalgae by osmotic shock method. In this study, osmotic shock method was going to be integrated with ultrasound to maximalize the extraction yield of lipid and protein from wet biomass Spirulina sp. with osmotic shock method assisted ultrasound. This study consisted of two steps, these were osmotic shock process toward wet biomass and ultrasound extraction assisted. NaCl solution was used as osmotic agent, with the variation of concentrations were 10%, 20%, and 30%. Extraction was conducted in 40°C for 20 minutes with frequency of ultrasound wave was 40kHz. The optimal yield of protein (2.7%) and (lipid 38%) were achieved at 20% osmotic agent concentration. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=extraction" title="extraction">extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=lipid" title=" lipid"> lipid</a>, <a href="https://publications.waset.org/abstracts/search?q=osmotic%20shock" title=" osmotic shock"> osmotic shock</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=ultrasound" title=" ultrasound"> ultrasound</a> </p> <a href="https://publications.waset.org/abstracts/76886/protein-and-lipid-extraction-from-microalgae-with-ultrasound-assisted-osmotic-shock-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/76886.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">359</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4234</span> Protein Extraction by Enzyme-Assisted Extraction followed by Alkaline Extraction from Red Seaweed Eucheuma denticulatum (Spinosum) Used in Carrageenan Production </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alireza%20Naseri">Alireza Naseri</a>, <a href="https://publications.waset.org/abstracts/search?q=Susan%20L.%20Holdt"> Susan L. Holdt</a>, <a href="https://publications.waset.org/abstracts/search?q=Charlotte%20Jacobsen"> Charlotte Jacobsen</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In 2014, the global amount of carrageenan production was 60,000 ton with a value of US$ 626 million. From this number, it can be estimated that the total dried seaweed consumption for this production was at least 300,000 ton/year. The protein content of these types of seaweed is 5 – 25%. If just half of this total amount of protein could be extracted, 18,000 ton/year of a high-value protein product would be obtained. The overall aim of this study was to develop a technology that will ensure further utilization of the seaweed that is used only as raw materials for carrageenan production as single extraction at present. More specifically, proteins should be extracted from the seaweed either before or after extraction of carrageenan with focus on maintaining the quality of carrageenan as a main product. Different mechanical, chemical and enzymatic technologies were evaluated. The optimized process was implemented in lab scale and based on its results; the new experiments were done a pilot and larger scale. In order to calculate the efficiency of the new upstream multi-extraction process, protein content was tested before and after extraction. After this step, the extraction of carrageenan was done and carrageenan content and the effect of extraction on yield were evaluated. The functionality and quality of carrageenan were measured based on rheological parameters. The results showed that by using the new multi-extraction process (submitted patent); it is possible to extract almost 50% of total protein without any negative impact on the carrageenan quality. Moreover, compared to the routine carrageenan extraction process, the new multi-extraction process could increase the yield of carrageenan and the rheological properties such as gel strength in the final carrageenan had a promising improvement. The extracted protein has initially been screened as a plant protein source in typical food applications. Further work will be carried out in order to improve properties such as color, solubility, and taste. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=carrageenan" title="carrageenan">carrageenan</a>, <a href="https://publications.waset.org/abstracts/search?q=extraction" title=" extraction"> extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=seaweed" title=" seaweed"> seaweed</a> </p> <a href="https://publications.waset.org/abstracts/89064/protein-extraction-by-enzyme-assisted-extraction-followed-by-alkaline-extraction-from-red-seaweed-eucheuma-denticulatum-spinosum-used-in-carrageenan-production" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/89064.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">284</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4233</span> Protein Isolates from Chickpea (Cicer arietinum L.) and Its Application in Cake</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohamed%20Abdullah%20Ahmed">Mohamed Abdullah Ahmed</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In a study of chickpea protein isolate (CPI) preparation, the wet alkaline extraction was carried out. The objectives were to determine the optimal extracting conditions of CPI and apply CPI into a sponge cake recipe to replace egg and make acceptable product. The design used in extraction was a central composite design. The response surface methodology was preferred to graphically express the relationship between extraction time and pH with the output variables of percent yield and protein content of CPI. It was noted that optimal extracting conditions were 60 min and pH 10.5 resulting in 90.07% protein content and 89.15% yield of CPI. The protein isolate (CPI) could be incorporated in cake to 20% without adversely affecting the cake physical properties such as cake hardness and sensory attributes. The higher protein content in cake was corresponding to the amount of CPI added. Therefore, adding CPI can significantly (p<0.05) increase protein content in cake. However, sensory evaluation showed that adding more than 20% of CPI decreased the overall acceptability. The results of this investigation could be used as a basic knowledge of CPI utilization in other food products. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chick%20bean%20protein%20isolate" title="chick bean protein isolate">chick bean protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=sponge%20cake" title=" sponge cake"> sponge cake</a>, <a href="https://publications.waset.org/abstracts/search?q=utilization" title=" utilization"> utilization</a>, <a href="https://publications.waset.org/abstracts/search?q=sponge" title=" sponge "> sponge </a> </p> <a href="https://publications.waset.org/abstracts/10335/protein-isolates-from-chickpea-cicer-arietinum-l-and-its-application-in-cake" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/10335.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">366</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4232</span> Use RP-HPLC To Investigate Factors Influencing Sorghum Protein Extraction</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Khaled%20Khaladi">Khaled Khaladi</a>, <a href="https://publications.waset.org/abstracts/search?q=Rafika%20Bibi"> Rafika Bibi</a>, <a href="https://publications.waset.org/abstracts/search?q=Hind%20Mokrane"> Hind Mokrane</a>, <a href="https://publications.waset.org/abstracts/search?q=Boubekeur%20Nadjemi"> Boubekeur Nadjemi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Sorghum (Sorghum bicolor (L.) Moench) is an important cereal crop grown in the semi-arid tropics of Africa and Asia due to its drought tolerance. Sorghum grain has protein content varying from 6 to 18%, with an average of 11%, Sorghum proteins can be broadly classified into prolamin and non-prolamin proteins. Kafirins, the major storage proteins, are classified as prolamins, and as such, they contain high levels of proline and glutamine and are soluble in non-polar solvents such as aqueous alcohols. Kafirins account for 77 to 82% of the protein in the endosperm, whereas non-prolamin proteins (namely, albumins, globulins, and glutelins) make up about 30% of the proteins. To optimize the extraction of sorghum proteins, several variables were examined: detergent type and concentration, reducing agent type and concentration, and buffer pH and concentration. Samples were quantified and characterized by RP-HPLC. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=sorghum" title="sorghum">sorghum</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20extraction" title=" protein extraction"> protein extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=detergent" title=" detergent"> detergent</a>, <a href="https://publications.waset.org/abstracts/search?q=food%20science" title=" food science "> food science </a> </p> <a href="https://publications.waset.org/abstracts/2669/use-rp-hplc-to-investigate-factors-influencing-sorghum-protein-extraction" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2669.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">320</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4231</span> Functionality and Application of Rice Bran Protein Hydrolysates in Oil in Water Emulsions: Their Stabilities to Environmental Stresses</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=R.%20Charoen">R. Charoen</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20Tipkanon"> S. Tipkanon</a>, <a href="https://publications.waset.org/abstracts/search?q=W.%20Savedboworn"> W. Savedboworn</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20Phonsatta"> N. Phonsatta</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Panya"> A. Panya</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Rice bran protein hydrolysates (RBPH) were prepared from defatted rice bran of two different Thai rice cultivars (Plai-Ngahm-Prachinburi; PNP and Khao Dok Mali 105; KDM105) using an enzymatic method. This research aimed to optimize enzyme-assisted protein extraction. In addition, the functional properties of RBPH and their stabilities to environmental stresses including pH (3 to 8), ionic strength (0 mM to 500 mM) and the thermal treatment (30 °C to 90 °C) were investigated. Results showed that enzymatic process for protein extraction of defatted rice bran was as follows: enzyme concentration 0.075 g/ 5 g of protein, extraction temperature 50 °C and extraction time 4 h. The obtained protein hydrolysate powders had a degree of hydrolysis (%) of 21.05% in PNP and 19.92% in KDM105. The solubility of protein hydrolysates at pH 4-6 was ranged from 27.28-38.57% and 27.60-43.00% in PNP and KDM105, respectively. In general, antioxidant activities indicated by total phenolic content, FRAP, ferrous ion-chelating (FIC), and 2,2’-azino-bis-3-ethylbenzthiazoline-6-sulphonic acid (ABTS) of KDM105 had higher than PNP. In terms of functional properties, the emulsifying activity index (EAI) was was 8.78 m²/g protein in KDM105, whereas PNP was 5.05 m²/g protein. The foaming capacity at 5 minutes (%) was 47.33 and 52.98 in PNP and KDM105, respectively. Glutamine, Alanine, Valine, and Leucine are the major amino acid in protein hydrolysates where the total amino acid of KDM105 gave higher than PNP. Furthermore, we investigated environmental stresses on the stability of 5% oil in water emulsion (5% oil, 10 mM citrate buffer) stabilized by RBPH (3.5%). The droplet diameter of emulsion stabilized by KDM105 was smaller (d < 250 nm) than produced by PNP. For environmental stresses, RBPH stabilized emulsions were stable at pH around 3 and 5-6, at high salt (< 400 mM, pH 7) and at temperatures range between 30-50°C. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=functional%20properties" title="functional properties">functional properties</a>, <a href="https://publications.waset.org/abstracts/search?q=oil%20in%20water%20emulsion" title=" oil in water emulsion"> oil in water emulsion</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20hydrolysates" title=" protein hydrolysates"> protein hydrolysates</a>, <a href="https://publications.waset.org/abstracts/search?q=rice%20bran%20protein" title=" rice bran protein"> rice bran protein</a> </p> <a href="https://publications.waset.org/abstracts/82295/functionality-and-application-of-rice-bran-protein-hydrolysates-in-oil-in-water-emulsions-their-stabilities-to-environmental-stresses" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/82295.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">218</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4230</span> Quality Rabbit Skin Gelatin with Acetic Acid Extract</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Wehandaka%20Pancapalaga">Wehandaka Pancapalaga</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study aimed to analyze the water content, yield, fat content, protein content, viscosity, gel strength, pH, melting and organoleptic rabbit skin gelatin with acetic acid extraction levels are different. The materials used in this study were Rex rabbit skin male. Treatments that P1 = the extraction of acetic acid 2% (v / v); P2 = the extraction of acetic acid 3% (v / v); P3 = the extraction of acetic acid 4 % (v / v). P5 = the extraction of acetic acid 5% (v / v). The results showed that the greater the concentration of acetic acid as the extraction of rabbit skin can reduce the water content and fat content of rabbit skin gelatin but increase the protein content, viscosity, pH, gel strength, yield and melting point rabbit skin gelatin. texture, color and smell of gelatin rabbits there were no differences with cow skin gelatin. The results showed that the quality of rabbit skin gelatin accordance Indonesian National Standard (SNI). Conclusion 5% acetic acid extraction produces the best quality gelatin. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=gelatin" title="gelatin">gelatin</a>, <a href="https://publications.waset.org/abstracts/search?q=skin%20rabbit" title=" skin rabbit"> skin rabbit</a>, <a href="https://publications.waset.org/abstracts/search?q=acetic%20acid%20extraction" title=" acetic acid extraction"> acetic acid extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=quality" title=" quality"> quality</a> </p> <a href="https://publications.waset.org/abstracts/61347/quality-rabbit-skin-gelatin-with-acetic-acid-extract" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/61347.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">417</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4229</span> Improvement of Protein Extraction From Shrimp by Product Used for Electrospinning by Applying Emerging Technologies</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mario%20P%C3%A9rez-Won">Mario Pérez-Won</a>, <a href="https://publications.waset.org/abstracts/search?q=Vilbett%20Briones%20L."> Vilbett Briones L.</a>, <a href="https://publications.waset.org/abstracts/search?q=Guido%20Trautmann"> Guido Trautmann</a>, <a href="https://publications.waset.org/abstracts/search?q=Mar%C3%ADa%20Jos%C3%A9%20Bugue%C3%B1o"> María José Bugueño</a>, <a href="https://publications.waset.org/abstracts/search?q=Gipsy%20Tabilo-Munizaga"> Gipsy Tabilo-Munizaga</a>, <a href="https://publications.waset.org/abstracts/search?q=Luis%20Gonzalez-Cavieres"> Luis Gonzalez-Cavieres</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The fishing industry generates a significant amount of shrimp byproducts, which often result in environmental contamination. Protein extraction from these by-products is a potential solution to minimize waste and revalue the by-products. To improve the extraction of proteins (by chemical method) from shrimp (Pleuroncodes monodon) by-products, the emerging technologies of ohmic heating (OH), microwaves (MW) and pulsed electric fields (PEF) were used. The results show that microwaves, electrical pulses, and ohmic heating improved performance by 28.19%, 19.25%, and 3.65%, respectively. Furthermore, conformational changes were studied by DSC and FTIR. Subsequently, the use of these proteins in electrospinning technology was evaluated. In conclusion, this study demonstrates that the application of emerging technologies, can significantly improve the extraction yield of proteins from shrimp by-products. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=electrospinning" title="electrospinning">electrospinning</a>, <a href="https://publications.waset.org/abstracts/search?q=emerging%20technologies" title=" emerging technologies"> emerging technologies</a>, <a href="https://publications.waset.org/abstracts/search?q=improving%20extraction" title=" improving extraction"> improving extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=shrimp%20by-products" title=" shrimp by-products"> shrimp by-products</a> </p> <a href="https://publications.waset.org/abstracts/170663/improvement-of-protein-extraction-from-shrimp-by-product-used-for-electrospinning-by-applying-emerging-technologies" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/170663.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">77</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4228</span> Functionalized Magnetic Iron Oxide Nanoparticles for Extraction of Protein and Metal Nanoparticles from Complex Fluids</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Meenakshi%20Verma">Meenakshi Verma</a>, <a href="https://publications.waset.org/abstracts/search?q=Mandeep%20Singh%20Bakshi"> Mandeep Singh Bakshi</a>, <a href="https://publications.waset.org/abstracts/search?q=Kultar%20Singh"> Kultar Singh</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Magnetic nanoparticles have received incredible importance in view of their diverse applications, which arise primarily due to their response to the external magnetic field. The magnetic behaviour of magnetic nanoparticles (NPs) helps them in numerous different ways. The most important amongst them is the ease with which they can be purified and also can be separated from the media in which they are present merely by applying an external magnetic field. This exceptional ease of separation of the magnetic NPs from an aqueous media enables them to use for extracting/removing metal pollutants from complex aqueous medium. Functionalized magnetic NPs can be subjected for the metallic impurities extraction if are favourably adsorbed on the NPs surfaces. We have successfully used the magnetic NPs as vehicles for gold and silver NPs removal from the complex fluids. The NPs loaded with gold and silver NPs pollutant fractions has been easily removed from the aqueous media by using external magnetic field. Similarly, we have used the magnetic NPs for extraction of protein from complex media and then constantly washed with pure water to eliminate the unwanted surface adsorbed components for quantitative estimation. The purified and protein loaded magnetic NPs are best analyzed with SDS Page to not only for characterization but also for separating the protein fractions. A collective review of the results indicates that we have synthesized surfactant coated iron oxide NPs and then functionalized these with selected materials. These surface active magnetic NPs work very well for the extraction of metallic NPs from the aqueous bulk and make the whole process environmentally sustainable. Also, magnetic NPs-Au/Ag/Pd hybrids have excellent protein extracting properties. They are much easier to use in order to extract the magnetic impurities as well as protein fractions under the effect of external magnetic field without any complex conventional purification methods. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=magnetic%20nanoparticles" title="magnetic nanoparticles">magnetic nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=functionalized" title=" functionalized"> functionalized</a>, <a href="https://publications.waset.org/abstracts/search?q=extraction" title=" extraction"> extraction</a> </p> <a href="https://publications.waset.org/abstracts/122882/functionalized-magnetic-iron-oxide-nanoparticles-for-extraction-of-protein-and-metal-nanoparticles-from-complex-fluids" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/122882.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">99</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4227</span> Isolation, Preparation and Biological Properties of Soybean-Flaxseed Protein Co-Precipitates</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Muhammad%20H.%20Alu%E2%80%99datt">Muhammad H. Alu’datt</a>, <a href="https://publications.waset.org/abstracts/search?q=Inteaz%20Alli"> Inteaz Alli</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study was conducted to prepare and evaluate the biological properties of protein co-precipitates from flaxseed and soybean. Protein was prepared by NaOH extraction through the mixing of soybean flour (Sf) and flaxseed flour (Ff) or mixtures of soybean extract (Se) and flaxseed extract (Fe). The protein co-precipitates were precipitated by isoelectric (IEP) and isoelectric-heating (IEPH) co-precipitation techniques. Effects of extraction and co-precipitation techniques on co-precipitate yield were investigated. Native-PAGE, SDS-PAGE were used to study the molecular characterization. Content and antioxidant activity of extracted free and bound phenolic compounds were evaluated for protein co-precipitates. Removal of free and bound phenolic compounds from protein co-precipitates showed little effects on the electrophoretic behavior of the proteins or the protein subunits of protein co-precipitates. Results showed that he highest protein contents and yield were obtained in for Sf-Ff/IEP co-precipitate with values of 53.28 and 25.58% respectively as compared to protein isolates and other co-precipitates. Results revealed that the Sf-Ff/IEP showed a higher content of bound phenolic compounds (53.49% from total phenolic content) as compared to free phenolic compounds (46.51% from total phenolic content). Antioxidant activities of extracted bound phenolic compounds with and without heat treatment from Sf-Ff/IEHP were higher as compared to free phenolic compounds extracted from other protein co-precipitates (29.68 and 22.84%, respectively). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=antioxidant" title="antioxidant">antioxidant</a>, <a href="https://publications.waset.org/abstracts/search?q=phenol" title=" phenol"> phenol</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20co-precipitate" title=" protein co-precipitate"> protein co-precipitate</a>, <a href="https://publications.waset.org/abstracts/search?q=yield" title=" yield"> yield</a> </p> <a href="https://publications.waset.org/abstracts/47994/isolation-preparation-and-biological-properties-of-soybean-flaxseed-protein-co-precipitates" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/47994.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">240</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4226</span> Extraction of Rice Bran Protein Using Enzymes and Polysaccharide Precipitation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sudarat%20Jiamyangyuen">Sudarat Jiamyangyuen</a>, <a href="https://publications.waset.org/abstracts/search?q=Tipawan%20Thongsook"> Tipawan Thongsook</a>, <a href="https://publications.waset.org/abstracts/search?q=Riantong%20Singanusong"> Riantong Singanusong</a>, <a href="https://publications.waset.org/abstracts/search?q=Chanida%20Saengtubtim"> Chanida Saengtubtim</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Rice is a staple food as well as exported commodity of Thailand. Rice bran, a 10.5% constituent of rice grain, is a by-product of rice milling process. Rice bran is normally used as a raw material for rice bran oil production or sold as feed with a low price. Therefore, this study aimed to increase value of defatted rice bran as obtained after extracting of rice bran oil. Conventionally, the protein in defatted rice bran was extracted using alkaline extraction and acid precipitation, which results in reduction of nutritious components in rice bran. Rice bran protein concentrate is suitable for those who are allergenic of protein from other sources eg. milk, wheat. In addition to its hypoallergenic property, rice bran protein also contains good quantity of lysine. Thus it may act as a suitable ingredient for infant food formulations while adding variety to the restricted diets of children with food allergies. The objectives of this study were to compare properties of rice bran protein concentrate (RBPC) extracted from defatted rice bran using enzymes together with precipitation step using polysaccharides (alginate and carrageenan) to those of a control sample extracted using a conventional method. The results showed that extraction of protein from rice bran using enzymes exhibited the higher protein recovery compared to that extraction with alkaline. The extraction conditions using alcalase 2% (v/w) at 50 C, pH 9.5 gave the highest protein (2.44%) and yield (32.09%) in extracted solution compared to other enzymes. Rice bran protein concentrate powder prepared by a precipitation step using alginate (protein in solution: alginate 1:0.006) exhibited the highest protein (27.55%) and yield (6.62%). Precipitation using alginate was better than that of acid. RBPC extracted with alkaline (ALK) or enzyme alcalase (ALC), then precipitated with alginate (AL) (samples RBP-ALK-AL and RBP-ALC-AL) yielded the precipitation rate of 75% and 91.30%, respectively. Therefore, protein precipitation using alginate was then selected. Amino acid profile of control sample, and sample precipitated with alginate, as compared to casein and soy protein isolated, showed that control sample showed the highest content among all sample. Functional property study of RBP showed that the highest nitrogen solubility occurred in pH 8-10. There was no statically significant between emulsion capacity and emulsion stability of control and sample precipitated by alginate. However, control sample showed a higher of foaming and lower foam stability compared to those of sample precipitated with alginate. The finding was successful in terms of minimizing chemicals used in extraction and precipitation steps in preparation of rice bran protein concentrate. This research involves in a production of value-added product in which the double amount of protein (28%) compared to original amount (14%) contained in rice bran could be beneficial in terms of adding to food products eg. healthy drink with high protein and fiber. In addition, the basic knowledge of functional property of rice bran protein concentrate was obtained, which can be used to appropriately select the application of this value-added product from rice bran. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alginate" title="alginate">alginate</a>, <a href="https://publications.waset.org/abstracts/search?q=carrageenan" title=" carrageenan"> carrageenan</a>, <a href="https://publications.waset.org/abstracts/search?q=rice%20bran" title=" rice bran"> rice bran</a>, <a href="https://publications.waset.org/abstracts/search?q=rice%20bran%20protein" title=" rice bran protein "> rice bran protein </a> </p> <a href="https://publications.waset.org/abstracts/26710/extraction-of-rice-bran-protein-using-enzymes-and-polysaccharide-precipitation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/26710.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">295</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4225</span> The Use of a Rabbit Model to Evaluate the Influence of Age on Excision Wound Healing</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=S.%20Bilal">S. Bilal</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20A.%20Bhat"> S. A. Bhat</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20Hussain"> I. Hussain</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20D.%20Parrah"> J. D. Parrah</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20P.%20Ahmad"> S. P. Ahmad</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20R.%20Mir"> M. R. Mir</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: The wound healing involves a highly coordinated cascade of cellular and immunological response over a period including coagulation, inflammation, granulation tissue formation, epithelialization, collagen synthesis and tissue remodeling. Wounds in aged heal more slowly than those in younger, mainly because of comorbidities that occur as one age. The present study is about the influence of age on wound healing. 1x1cm^2 (100 mm) wounds were created on the back of the animal. The animals were divided into two groups; one group had animals in the age group of 3-9 months while another group had animals in the age group of 15-21 months. Materials and Methods: 24 clinically healthy rabbits in the age group of 3-21 months were used as experimental animals and divided into two groups viz A and B. All experimental parameters, i.e., Excision wound model, Measurement of wound area, Protein extraction and estimation, Protein extraction and estimation and DNA extraction and estimation were done by standard methods. Results: The parameters studied were wound contraction, hydroxyproline, glucosamine, protein, and DNA. A significant increase (p<0.005) in the hydroxyproline, glucosamine, protein and DNA and a significant decrease in wound area (p<0.005) was observed in the age group of 3-9 months when compared to animals of an age group of 15-21 months. Wound contraction together with hydroxyproline, glucosamine, protein and DNA estimations suggest that advanced age results in retarded wound healing. Conclusion: The decrease wound contraction and accumulation of hydroxyproline, glucosamine, protein and DNA in group B animals may be associated with the reduction or delay in growth factors because of the advancing age. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=age" title="age">age</a>, <a href="https://publications.waset.org/abstracts/search?q=wound%20healing" title=" wound healing"> wound healing</a>, <a href="https://publications.waset.org/abstracts/search?q=excision%20wound" title=" excision wound"> excision wound</a>, <a href="https://publications.waset.org/abstracts/search?q=hydroxyproline" title=" hydroxyproline"> hydroxyproline</a>, <a href="https://publications.waset.org/abstracts/search?q=glucosamine" title=" glucosamine"> glucosamine</a> </p> <a href="https://publications.waset.org/abstracts/22034/the-use-of-a-rabbit-model-to-evaluate-the-influence-of-age-on-excision-wound-healing" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/22034.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">659</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4224</span> Integration of the Electro-Activation Technology for Soy Meal Valorization</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Natela%20Gerliani">Natela Gerliani</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohammed%20Aider"> Mohammed Aider</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Nowadays, the interest of using sustainable technologies for protein extraction from underutilized oilseeds is growing. Currently, a major disposal problem for the oil industry is by-products of plant food processing such as soybean meal. That is why valorization of soybean meal is important for the oil industry since it contains high-quality proteins and other valuable components. Generally, soybean meal is used in livestock and poultry feed but is rarely used in human feed. Though chemical composition of this meal compensate nutritional deficiency and can be used to balance protein in human food. Regarding the efficiency of soybean meal valorization, extraction is a key process for obtaining enriched protein ingredient, which can be incorporated into the food matrix. However, most of the food components such as proteins extracted from oilseeds by-products imply the utilization of organic and inorganic chemicals (e.g. acids, bases, TCA-acetone) having a significant environmental impact. In a context of sustainable production, the use of an electro-activation technology seems to be a good alternative. Indeed, the electro-activation technology requires only water, food grade salt and electricity as main materials. Moreover, this innovative technology helps to avoid special equipment and trainings for workers safety as well as transport and storage of hazardous materials. Electro-activation is a technology based on applied electrochemistry for the generation of acidic and alkaline solutions on the basis of the oxidation-reduction reactions that occur at the vicinity electrode/solution interfaces. It is an eco-friendly process that can be used to replace the conventional acidic and alkaline extraction. In this research, the electro-activation technology for protein extraction from soybean meal was carried out in the electro-activation reactor. This reactor consists of three compartments separated by cation and anion exchange membranes that allow creating non-contacting acidic and basic solutions. Different current intensities (150 mA, 300 mA and 450 mA) and treatment durations (10 min, 30 min and 50 min) were tested. The results showed that the extracts obtained by the electro-activation method have good quality in comparison to conventional extracts. For instance, extractability obtained with electro-activation method was 55% whereas with the conventional method it was only 36%. Moreover, a maximum protein quantity of 48 % in the extract was obtained with the electro-activation technology comparing to the maximum amount of protein obtained by conventional extraction of 41 %. Hence, the environmentally sustainable electro-activation technology seems to be a promising type of protein extraction that can replace conventional extraction technology. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=by-products" title="by-products">by-products</a>, <a href="https://publications.waset.org/abstracts/search?q=eco-friendly%20technology" title=" eco-friendly technology"> eco-friendly technology</a>, <a href="https://publications.waset.org/abstracts/search?q=electro-activation" title=" electro-activation"> electro-activation</a>, <a href="https://publications.waset.org/abstracts/search?q=soybean%20meal" title=" soybean meal"> soybean meal</a> </p> <a href="https://publications.waset.org/abstracts/89297/integration-of-the-electro-activation-technology-for-soy-meal-valorization" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/89297.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">228</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4223</span> Mechanisms of Ginger Bioactive Compounds Extract Using Soxhlet and Accelerated Water Extraction</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=M.%20N.%20Azian">M. N. Azian</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20N.%20Ilia%20Anisa"> A. N. Ilia Anisa</a>, <a href="https://publications.waset.org/abstracts/search?q=Y.%20Iwai"> Y. Iwai</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The mechanism for extraction bioactive compounds from plant matrix is essential for optimizing the extraction process. As a benchmark technique, a soxhlet extraction has been utilized for discussing the mechanism and compared with an accelerated water extraction. The trends of both techniques show that the process involves extraction and degradation. The highest yields of 6-, 8-, 10-gingerols and 6-shogaol in soxhlet extraction were 13.948, 7.12, 10.312 and 2.306 mg/g, respectively. The optimum 6-, 8-, 10-gingerols and 6-shogaol extracted by the accelerated water extraction at 140oC were 68.97±3.95 mg/g at 3min, 18.98±3.04 mg/g at 5min, 5.167±2.35 mg/g at 3min and 14.57±6.27 mg/g at 3min, respectively. The effect of temperature at 3mins shows that the concentration of 6-shogaol increased rapidly as decreasing the recovery of 6-gingerol. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=mechanism" title="mechanism">mechanism</a>, <a href="https://publications.waset.org/abstracts/search?q=ginger%20bioactive%20compounds" title=" ginger bioactive compounds"> ginger bioactive compounds</a>, <a href="https://publications.waset.org/abstracts/search?q=soxhlet%20extraction" title=" soxhlet extraction"> soxhlet extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=accelerated%20water%20extraction" title=" accelerated water extraction"> accelerated water extraction</a> </p> <a href="https://publications.waset.org/abstracts/9278/mechanisms-of-ginger-bioactive-compounds-extract-using-soxhlet-and-accelerated-water-extraction" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/9278.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">434</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4222</span> Hydration of Protein-RNA Recognition Sites</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Amita%20Barik">Amita Barik</a>, <a href="https://publications.waset.org/abstracts/search?q=Ranjit%20Prasad%20Bahadur"> Ranjit Prasad Bahadur</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We investigate the role of water molecules in 89 protein-RNA complexes taken from the Protein Data Bank. Those with tRNA and single-stranded RNA are less hydrated than with duplex or ribosomal proteins. Protein-RNA interfaces are hydrated less than protein-DNA interfaces, but more than protein-protein interfaces. Majority of the waters at protein-RNA interfaces makes multiple H-bonds; however, a fraction does not make any. Those making Hbonds have preferences for the polar groups of RNA than its partner protein. The spatial distribution of waters makes interfaces with ribosomal proteins and single-stranded RNA relatively ‘dry’ than interfaces with tRNA and duplex RNA. In contrast to protein-DNA interfaces, mainly due to the presence of the 2’OH, the ribose in protein-RNA interfaces is hydrated more than the phosphate or the bases. The minor groove in protein-RNA interfaces is hydrated more than the major groove, while in protein-DNA interfaces it is reverse. The strands make the highest number of water-mediated H-bonds per unit interface area followed by the helices and the non-regular structures. The preserved waters at protein-RNA interfaces make higher number of H-bonds than the other waters. Preserved waters contribute toward the affinity in protein-RNA recognition and should be carefully treated while engineering protein-RNA interfaces. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=h-bonds" title="h-bonds">h-bonds</a>, <a href="https://publications.waset.org/abstracts/search?q=minor-major%20grooves" title=" minor-major grooves"> minor-major grooves</a>, <a href="https://publications.waset.org/abstracts/search?q=preserved%20water" title=" preserved water"> preserved water</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-RNA%20interfaces" title=" protein-RNA interfaces"> protein-RNA interfaces</a> </p> <a href="https://publications.waset.org/abstracts/42932/hydration-of-protein-rna-recognition-sites" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/42932.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">302</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4221</span> Functional Properties of Sunflower Protein Concentrates Extracted Using Different Anti-greening Agents - Low-Fat Whipping Cream Preparation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tamer%20M.%20El-Messery">Tamer M. El-Messery</a> </p> <p class="card-text"><strong>Abstract:</strong></p> By-products from sunflower oil extraction, such as sunflower cakes, are rich sources of proteins with desirable functional properties for the food industry. However, challenges such as sensory drawbacks and the presence of phenolic compounds have hindered their widespread use. In this study, sunflower protein concentrates were obtained from sunflower cakes using different ant-greening solvents (ascorbic acid (ASC) and N-acetylcysteine (NAC)), and their functional properties were evaluated. The color of extracted proteins ranged from dark green to yellow, where the using of ASC and NAC agents enhanced the color. The protein concentrates exhibited high solubility (>70%) and antioxidant activity, with hydrophobicity influencing emulsifying activity. Emulsions prepared with these proteins showed stability and microencapsulation efficiency. Incorporation of protein concentrates into low-fat whipping cream formulations increased overrun and affected color characteristics. Rheological studies demonstrated pseudoplastic behavior in whipped cream, influenced by shear rates and protein content. Overall, sunflower protein isolates showed promising functional properties, indicating their potential as valuable ingredients in food formulations. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=functional%20properties" title="functional properties">functional properties</a>, <a href="https://publications.waset.org/abstracts/search?q=sunflower%20protein%20concentrates" title=" sunflower protein concentrates"> sunflower protein concentrates</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20capacity" title=" antioxidant capacity"> antioxidant capacity</a>, <a href="https://publications.waset.org/abstracts/search?q=ant-greening%20agents" title=" ant-greening agents"> ant-greening agents</a>, <a href="https://publications.waset.org/abstracts/search?q=low-fat%20whipping%20cream" title=" low-fat whipping cream"> low-fat whipping cream</a> </p> <a href="https://publications.waset.org/abstracts/185953/functional-properties-of-sunflower-protein-concentrates-extracted-using-different-anti-greening-agents-low-fat-whipping-cream-preparation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/185953.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">48</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4220</span> Extraction of Phycocyanin from Spirulina platensis by Isoelectric Point Precipitation and Salting Out for Scale Up Processes</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Velasco-Rend%C3%B3n%20Mar%C3%ADa%20Del%20Carmen">Velasco-Rendón María Del Carmen</a>, <a href="https://publications.waset.org/abstracts/search?q=Cu%C3%A9llar-Berm%C3%BAdez%20Sara%20Paulina"> Cuéllar-Bermúdez Sara Paulina</a>, <a href="https://publications.waset.org/abstracts/search?q=Parra-Sald%C3%ADvar%20Roberto"> Parra-Saldívar Roberto</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Phycocyanin is a blue pigment protein with fluorescent activity produced by cyanobacteria. It has been recently studied to determine its anticancer, antioxidant and antiinflamatory potential. Since 2014 it was approved as a Generally Recognized As Safe (GRAS) proteic pigment for the food industry. Therefore, phycocyanin shows potential for the food, nutraceutical, pharmaceutical and diagnostics industry. Conventional phycocyanin extraction includes buffer solutions and ammonium sulphate followed by chromatography or ATPS for protein separation. Therefore, further purification steps are time-requiring, energy intensive and not suitable for scale-up processing. This work presents an alternative to conventional methods that also allows large scale application with commercially available equipment. The extraction was performed by exposing the dry biomass to mechanical cavitation and salting out with NaCl to use an edible reagent. Also, isoelectric point precipitation was used by addition of HCl and neutralization with NaOH. The results were measured and compared in phycocyanin concentration, purity and extraction yield. Results showed that the best extraction condition was the extraction by salting out with 0.20 M NaCl after 30 minutes cavitation, with a concentration in the supernatant of 2.22 mg/ml, a purity of 3.28 and recovery from crude extract of 81.27%. Mechanical cavitation presumably increased the solvent-biomass contact, making the crude extract visibly dark blue after centrifugation. Compared to other systems, our process has less purification steps, similar concentrations in the phycocyanin-rich fraction and higher purity. The contaminants present in our process edible NaCl or low pHs that can be neutralized. It also can be adapted to a semi-continuous process with commercially available equipment. This characteristics make this process an appealing alternative for phycocyanin extraction as a pigment for the food industry. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=extraction" title="extraction">extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=phycocyanin" title=" phycocyanin"> phycocyanin</a>, <a href="https://publications.waset.org/abstracts/search?q=precipitation" title=" precipitation"> precipitation</a>, <a href="https://publications.waset.org/abstracts/search?q=scale-up" title=" scale-up"> scale-up</a> </p> <a href="https://publications.waset.org/abstracts/27087/extraction-of-phycocyanin-from-spirulina-platensis-by-isoelectric-point-precipitation-and-salting-out-for-scale-up-processes" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/27087.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">438</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4219</span> Protein Crystallization Induced by Surface Plasmon Resonance</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tetsuo%20Okutsu">Tetsuo Okutsu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We have developed a crystallization plate with the function of promoting protein crystallization. A gold thin film is deposited on the crystallization plate. A protein solution is dropped thereon, and crystallization is promoted when the protein is irradiated with light of a wavelength that protein does not absorb. Protein is densely adsorbed on the gold thin film surface. The light excites the surface plasmon resonance of the gold thin film, the protein is excited by the generated enhanced electric field induced by surface plasmon resonance, and the amino acid residues are radicalized to produce protein dimers. The dimers function as templates for protein crystals, crystallization is promoted. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=lysozyme" title="lysozyme">lysozyme</a>, <a href="https://publications.waset.org/abstracts/search?q=plasmon" title=" plasmon"> plasmon</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=crystallization" title=" crystallization"> crystallization</a>, <a href="https://publications.waset.org/abstracts/search?q=RNaseA" title=" RNaseA"> RNaseA</a> </p> <a href="https://publications.waset.org/abstracts/85433/protein-crystallization-induced-by-surface-plasmon-resonance" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/85433.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">218</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4218</span> Oil Extraction from Microalgae Dunalliela sp. by Polar and Non-Polar Solvents</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20Zonouzi">A. Zonouzi</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Auli"> M. Auli</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Javanmard%20Dakheli"> M. Javanmard Dakheli</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20A.%20Hejazi"> M. A. Hejazi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Microalgae are tiny photosynthetic plants. Nowadays, microalgae are being used as nutrient-dense foods and sources of fine chemicals. They have significant amounts of lipid, carotenoids, vitamins, protein, minerals, chlorophyll, and pigments. Oil extraction from algae is a hotly debated topic currently because introducing an efficient method could decrease the process cost. This can determine the sustainability of algae-based foods. Scientific research works show that solvent extraction using chloroform/methanol (2:1) mixture is one of the efficient methods for oil extraction from algal cells, but both methanol and chloroform are toxic solvents, and therefore, the extracted oil will not be suitable for food application. In this paper, the effect of two food grade solvents (hexane and hexane/ isopropanol) on oil extraction yield from microalgae <em>Dunaliella </em>sp. was investigated and the results were compared with chloroform/methanol (2:1) extraction yield. It was observed that the oil extraction yield using hexane, hexane/isopropanol (3:2) and chloroform/methanol (2:1) mixture were 5.4, 13.93, and 17.5 (% w/w, dry basis), respectively. The fatty acid profile derived from GC illustrated that the palmitic (36.62%), oleic (18.62%), and stearic acids (19.08%) form the main portion of fatty acid composition of microalgae <em>Dunalliela </em>sp. oil. It was concluded that, the addition of isopropanol as polar solvent could increase the extraction yield significantly. Isopropanol solves cell wall phospholipids and enhances the release of intercellular lipids, which improves accessing of hexane to fatty acids. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=fatty%20acid%20profile%E2%80%8E" title="fatty acid profile‎">fatty acid profile‎</a>, <a href="https://publications.waset.org/abstracts/search?q=microalgae%E2%80%8E" title=" microalgae‎"> microalgae‎</a>, <a href="https://publications.waset.org/abstracts/search?q=oil%20extraction%E2%80%8E" title=" oil extraction‎"> oil extraction‎</a>, <a href="https://publications.waset.org/abstracts/search?q=polar%20solvent%E2%80%8E" title=" polar solvent‎"> polar solvent‎</a> </p> <a href="https://publications.waset.org/abstracts/56505/oil-extraction-from-microalgae-dunalliela-sp-by-polar-and-non-polar-solvents" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/56505.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">376</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4217</span> Identification and Characterization of Nuclear Envelope Protein Interactions</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohammed%20Hakim%20Jafferali">Mohammed Hakim Jafferali</a>, <a href="https://publications.waset.org/abstracts/search?q=Balaje%20Vijayaraghavan"> Balaje Vijayaraghavan</a>, <a href="https://publications.waset.org/abstracts/search?q=Ricardo%20A.%20Figueroa"> Ricardo A. Figueroa</a>, <a href="https://publications.waset.org/abstracts/search?q=Ellinor%20Crafoord"> Ellinor Crafoord</a>, <a href="https://publications.waset.org/abstracts/search?q=Veronica%20J.%20Larsson"> Veronica J. Larsson</a>, <a href="https://publications.waset.org/abstracts/search?q=Einar%20Hallberg"> Einar Hallberg</a>, <a href="https://publications.waset.org/abstracts/search?q=Santhosh%20Gudise"> Santhosh Gudise </a> </p> <p class="card-text"><strong>Abstract:</strong></p> The nuclear envelope which surrounds the chromatin of eukaryotic cells contains more than a hundred transmembrane proteins. Mutations in some genes encoding nuclear envelope proteins give rise to human diseases including neurological disorders. The function of many nuclear envelope proteins is not well established. This is partly because nuclear envelope proteins and their interactions are difficult to study due to the inherent resistance to extraction of nuclear envelope proteins. We have developed a novel method called MCLIP, to identify interacting partners of nuclear envelope proteins in live cells. Using MCLIP, we found three new binding partners of the inner nuclear membrane protein Samp1: the intermediate filament protein Lamin B1, the LINC complex protein Sun1 and the G-protein Ran. Furthermore, using in vitro studies, we show that Samp1 binds both Emerin and Ran directly. We have also studied the interaction between Samp1 and Ran in detail. The results show that the Samp1 binds stronger to RanGTP than RanGDP. Samp1 is the first transmembrane protein known to bind Ran and it is tempting to speculate that Samp1 may provide local binding sites for RanGTP at membranes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=MCLIP" title="MCLIP">MCLIP</a>, <a href="https://publications.waset.org/abstracts/search?q=nuclear%20envelope" title=" nuclear envelope"> nuclear envelope</a>, <a href="https://publications.waset.org/abstracts/search?q=ran" title=" ran"> ran</a>, <a href="https://publications.waset.org/abstracts/search?q=Samp1" title=" Samp1"> Samp1</a> </p> <a href="https://publications.waset.org/abstracts/42955/identification-and-characterization-of-nuclear-envelope-protein-interactions" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/42955.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">353</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4216</span> Protein Remote Homology Detection and Fold Recognition by Combining Profiles with Kernel Methods</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bin%20Liu">Bin Liu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Protein remote homology detection and fold recognition are two most important tasks in protein sequence analysis, which is critical for protein structure and function studies. In this study, we combined the profile-based features with various string kernels, and constructed several computational predictors for protein remote homology detection and fold recognition. Experimental results on two widely used benchmark datasets showed that these methods outperformed the competing methods, indicating that these predictors are useful computational tools for protein sequence analysis. By analyzing the discriminative features of the training models, some interesting patterns were discovered, reflecting the characteristics of protein superfamilies and folds, which are important for the researchers who are interested in finding the patterns of protein folds. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20remote%20homology%20detection" title="protein remote homology detection">protein remote homology detection</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20fold%20recognition" title=" protein fold recognition"> protein fold recognition</a>, <a href="https://publications.waset.org/abstracts/search?q=profile-based%20features" title=" profile-based features"> profile-based features</a>, <a href="https://publications.waset.org/abstracts/search?q=Support%20Vector%20Machines%20%28SVMs%29" title=" Support Vector Machines (SVMs)"> Support Vector Machines (SVMs)</a> </p> <a href="https://publications.waset.org/abstracts/104054/protein-remote-homology-detection-and-fold-recognition-by-combining-profiles-with-kernel-methods" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/104054.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">161</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4215</span> Analytical Study of Cobalt(II) and Nickel(II) Extraction with Salicylidene O-, M-, and P-Toluidine in Chloroform</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sana%20Almi">Sana Almi</a>, <a href="https://publications.waset.org/abstracts/search?q=Djamel%20Barkat"> Djamel Barkat </a> </p> <p class="card-text"><strong>Abstract:</strong></p> The solvent extraction of cobalt (II) and nickel (II) from aqueous sulfate solutions were investigated with the analytical methods of slope analysis using salicylidene aniline and the three isomeric o-, m- and p-salicylidene toluidine diluted with chloroform at 25°C. By a statistical analysis of the extraction data, it was concluded that the extracted species are CoL2 with CoL2(HL) and NiL2 (HL denotes HSA, HSOT, HSMT, and HSPT). The extraction efficiency of Co(II) was higher than Ni(II). This tendency is confirmed from numerical extraction constants for each metal cations. The best extraction was according to the following order: HSMT > HSPT > HSOT > HSA for Co2+ and Ni2+. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=solvent%20extraction" title="solvent extraction">solvent extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=nickel%28II%29" title=" nickel(II)"> nickel(II)</a>, <a href="https://publications.waset.org/abstracts/search?q=cobalt%28II%29" title=" cobalt(II)"> cobalt(II)</a>, <a href="https://publications.waset.org/abstracts/search?q=salicylidene%20aniline" title=" salicylidene aniline"> salicylidene aniline</a>, <a href="https://publications.waset.org/abstracts/search?q=o-" title=" o-"> o-</a>, <a href="https://publications.waset.org/abstracts/search?q=m-" title=" m-"> m-</a>, <a href="https://publications.waset.org/abstracts/search?q=and%20p-salicylidene%20toluidine" title=" and p-salicylidene toluidine"> and p-salicylidene toluidine</a> </p> <a href="https://publications.waset.org/abstracts/21677/analytical-study-of-cobaltii-and-nickelii-extraction-with-salicylidene-o-m-and-p-toluidine-in-chloroform" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/21677.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">485</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4214</span> A Comparative Study of the Physicochemical and Structural Properties of Quinoa Protein Isolate and Yellow Squat Shrimp Byproduct Protein Isolate through pH-Shifting Modification</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mar%C3%ADa%20Jos%C3%A9%20Bugue%C3%B1o">María José Bugueño</a>, <a href="https://publications.waset.org/abstracts/search?q=Natalia%20Jaime"> Natalia Jaime</a>, <a href="https://publications.waset.org/abstracts/search?q=Cristian%20Castro"> Cristian Castro</a>, <a href="https://publications.waset.org/abstracts/search?q=Diego%20Naranjo"> Diego Naranjo</a>, <a href="https://publications.waset.org/abstracts/search?q=Guido%20Trautmann"> Guido Trautmann</a>, <a href="https://publications.waset.org/abstracts/search?q=Mario%20P%C3%A9rez-Won"> Mario Pérez-Won</a>, <a href="https://publications.waset.org/abstracts/search?q=Vilbett%20Briones-Labarca"> Vilbett Briones-Labarca</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Proteins play a crucial role in various prepared foods, including dairy products, drinks, emulsions, and ready meals. These food proteins are naturally present in food waste and byproducts. The alkaline extraction and acid precipitation method is commonly used to extract proteins from plants and animals due to its product stability, cost-effectiveness, and ease of use. This study aimed to investigate the impact of pH-shifting storage at two different pH levels on the conformational changes affecting the physicochemical and functional properties of quinoa protein isolate (QPI) and yellow shrimp byproduct protein isolate (YSPI). The QPI and YSPI were extracted using the alkaline extraction-isoelectric precipitation method. The dispersions were adjusted to pH 4 or 12, stirred for 2 hours at 20°C to achieve a uniform dispersion, and then freeze-dried. Various analyses were conducted, including flexibility (F), free sulfhydryl content (Ho), emulsifying activity (EA), emulsifying capacity (EC), water holding capacity (WHC), oil holding capacity (OHC), intrinsic fluorescence, ultraviolet spectroscopy, differential scanning calorimetry (DSC), and Fourier transform infrared spectroscopy (FTIR) to assess the properties of the protein isolates. pH-shifting at pH 11 and 12 for QPI and YSPI, respectively, significantly improved protein properties, while property modification of the samples treated under acidic conditions was less pronounced. Additionally, the pH 11 and 12 treatments significantly improved F, Ho, EA, WHC, OHC, intrinsic fluorescence, ultraviolet spectroscopy, DSC, and FTIR. The increase in Ho was due to disulfide bond disruption, which produced more protein sub-units than other treatments for both proteins. This study provides theoretical support for comprehensively elucidating the functional properties of protein isolates, promoting the application of plant proteins and marine byproducts. The pH-shifting process effectively improves the emulsifying property and stability of QPI and YSPI, which can be considered potential plant-based or marine byproduct-based emulsifiers for use in the food industry. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=quinoa%20protein" title="quinoa protein">quinoa protein</a>, <a href="https://publications.waset.org/abstracts/search?q=yellow%20shrimp%20by-product%20protein" title=" yellow shrimp by-product protein"> yellow shrimp by-product protein</a>, <a href="https://publications.waset.org/abstracts/search?q=physicochemical%20properties" title=" physicochemical properties"> physicochemical properties</a>, <a href="https://publications.waset.org/abstracts/search?q=structural%20properties" title=" structural properties"> structural properties</a> </p> <a href="https://publications.waset.org/abstracts/188225/a-comparative-study-of-the-physicochemical-and-structural-properties-of-quinoa-protein-isolate-and-yellow-squat-shrimp-byproduct-protein-isolate-through-ph-shifting-modification" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/188225.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">43</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4213</span> Jamun Juice Extraction Using Commercial Enzymes and Optimization of the Treatment with the Help of Physicochemical, Nutritional and Sensory Properties</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Payel%20Ghosh">Payel Ghosh</a>, <a href="https://publications.waset.org/abstracts/search?q=Rama%20Chandra%20Pradhan"> Rama Chandra Pradhan</a>, <a href="https://publications.waset.org/abstracts/search?q=Sabyasachi%20Mishra"> Sabyasachi Mishra</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Jamun (<em>Syzygium cuminii </em>L.) is one of the important indigenous minor fruit with high medicinal value. The jamun cultivation is unorganized and there is huge loss of this fruit every year. The perishable nature of the fruit makes its postharvest management further difficult. Due to the strong cell wall structure of pectin-protein bonds and hard seeds, extraction of juice becomes difficult. Enzymatic treatment has been commercially used for improvement of juice quality with high yield. The objective of the study was to optimize the best treatment method for juice extraction. Enzymes (Pectinase and Tannase) from different stains had been used and for each enzyme, best result obtained by using response surface methodology. Optimization had been done on the basis of physicochemical property, nutritional property, sensory quality and cost estimation. According to quality aspect, cost analysis and sensory evaluation, the optimizing enzymatic treatment was obtained by Pectinase from <em>Aspergillus aculeatus</em> strain. The optimum condition for the treatment was 44 <sup>o</sup>C with 80 minute with a concentration of 0.05% (w/w). At these conditions, 75% of yield with turbidity of 32.21NTU, clarity of 74.39%T, polyphenol content of 115.31 mg GAE/g, protein content of 102.43 mg/g have been obtained with a significant difference in overall acceptability. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=enzymatic%20treatment" title="enzymatic treatment">enzymatic treatment</a>, <a href="https://publications.waset.org/abstracts/search?q=Jamun" title=" Jamun"> Jamun</a>, <a href="https://publications.waset.org/abstracts/search?q=optimization" title=" optimization"> optimization</a>, <a href="https://publications.waset.org/abstracts/search?q=physicochemical%20property" title=" physicochemical property"> physicochemical property</a>, <a href="https://publications.waset.org/abstracts/search?q=sensory%20analysis" title=" sensory analysis"> sensory analysis</a> </p> <a href="https://publications.waset.org/abstracts/59901/jamun-juice-extraction-using-commercial-enzymes-and-optimization-of-the-treatment-with-the-help-of-physicochemical-nutritional-and-sensory-properties" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/59901.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">296</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4212</span> Extraction of Essential Oil From Orange Peels</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Aayush%20Bhisikar">Aayush Bhisikar</a>, <a href="https://publications.waset.org/abstracts/search?q=Neha%20Rajas"> Neha Rajas</a>, <a href="https://publications.waset.org/abstracts/search?q=Aditya%20Bhingare"> Aditya Bhingare</a>, <a href="https://publications.waset.org/abstracts/search?q=Samarth%20Bhandare"> Samarth Bhandare</a>, <a href="https://publications.waset.org/abstracts/search?q=Amruta%20Amrurkar"> Amruta Amrurkar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Orange peels are currently thrown away as garbage in India after orange fruits' edible components are consumed. However, the nation depends on important essential oils for usage in companies that produce goods, including food, beverages, cosmetics, and medicines. This study was conducted to show how to effectively use it. By using various extraction techniques, orange peel is used in the creation of essential oils. Stream distillation, water distillation, and solvent extraction were the techniques taken into consideration in this paper. Due to its relative prevalence among the extraction techniques, Design Expert 7.0 was used to plan an experimental run for solvent extraction. Oil was examined to ascertain its physical and chemical characteristics after extraction. It was determined from the outcomes that the orange peels. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=orange%20peels" title="orange peels">orange peels</a>, <a href="https://publications.waset.org/abstracts/search?q=extraction" title=" extraction"> extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=essential%20oil" title=" essential oil"> essential oil</a>, <a href="https://publications.waset.org/abstracts/search?q=distillation" title=" distillation"> distillation</a> </p> <a href="https://publications.waset.org/abstracts/173039/extraction-of-essential-oil-from-orange-peels" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/173039.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">87</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4211</span> Extraction of Essential Oil from Orange Peels</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Neha%20Rajas">Neha Rajas</a>, <a href="https://publications.waset.org/abstracts/search?q=Aayush%20Bhisikar"> Aayush Bhisikar</a>, <a href="https://publications.waset.org/abstracts/search?q=Samarth%20Bhandare"> Samarth Bhandare</a>, <a href="https://publications.waset.org/abstracts/search?q=Aditya%20Bhingare"> Aditya Bhingare</a>, <a href="https://publications.waset.org/abstracts/search?q=Amruta%20Amrutkar"> Amruta Amrutkar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Orange peels are currently thrown away as garbage in India after orange fruits' edible components are consumed. However, the nation depends on important essential oils for usage in companies that produce goods, including food, beverages, cosmetics, and medicines. This study was conducted to show how to effectively use it. By using various extraction techniques, orange peel is used in the creation of essential oils. Stream distillation, water distillation, and solvent extraction were the techniques taken into consideration in this paper. Due to its relative prevalence among the extraction techniques, Design Expert 7.0 was used to plan an experimental run for solvent extraction. Oil was examined to ascertain its physical and chemical characteristics after extraction. It was determined from the outcomes that the orange peels. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=orange%20peels" title="orange peels">orange peels</a>, <a href="https://publications.waset.org/abstracts/search?q=extraction" title=" extraction"> extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=distillation" title=" distillation"> distillation</a>, <a href="https://publications.waset.org/abstracts/search?q=essential%20oil" title=" essential oil"> essential oil</a> </p> <a href="https://publications.waset.org/abstracts/173321/extraction-of-essential-oil-from-orange-peels" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/173321.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">80</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4210</span> Membrane Spanning DNA Origami Nanopores for Protein Translocation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Genevieve%20Pugh">Genevieve Pugh</a>, <a href="https://publications.waset.org/abstracts/search?q=Johnathan%20Burns"> Johnathan Burns</a>, <a href="https://publications.waset.org/abstracts/search?q=Stefan%20Howorka"> Stefan Howorka</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Single-molecule sensing via protein nanopores has achieved a step-change in portable and label-free DNA sequencing. However, protein pores of both natural or engineered origin are not able to produce the tunable diameters needed for effective protein sensing. Here, we describe a generic strategy to build synthetic DNA nanopores that are wide enough to accommodate folded protein. The pores are composed of interlinked DNA duplexes and carry lipid anchors to achieve the required membrane insertion. Our demonstrator pore has a contiguous cross-sectional channel area of 50 nm2 which is 6-times larger than the largest protein pore. Consequently, transport of folded protein across bilayers is possible. The modular design is amenable for different pore dimensions and can be adapted for protein sensing or to create molecular gates in synthetic biology. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biosensing" title="biosensing">biosensing</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20nanotechnology" title=" DNA nanotechnology"> DNA nanotechnology</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20origami" title=" DNA origami"> DNA origami</a>, <a href="https://publications.waset.org/abstracts/search?q=nanopore%20sensing" title=" nanopore sensing"> nanopore sensing</a> </p> <a href="https://publications.waset.org/abstracts/78556/membrane-spanning-dna-origami-nanopores-for-protein-translocation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/78556.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">324</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4209</span> Microwave-Assisted Extraction of Lycopene from Gac Arils (Momordica cochinchinensis (Lour.) Spreng)</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Yardfon%20Tanongkankit">Yardfon Tanongkankit</a>, <a href="https://publications.waset.org/abstracts/search?q=Kanjana%20Narkprasom"> Kanjana Narkprasom</a>, <a href="https://publications.waset.org/abstracts/search?q=Nukrob%20Narkprasom"> Nukrob Narkprasom</a>, <a href="https://publications.waset.org/abstracts/search?q=Khwanruthai%20Saiupparat"> Khwanruthai Saiupparat</a>, <a href="https://publications.waset.org/abstracts/search?q=Phatthareeya%20Siriwat"> Phatthareeya Siriwat</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Gac fruit (Momordica cochinchinensis (Lour.) Spreng) possesses high potential for health food as it contains high lycopene contents. The objective of this study was to optimize the extraction of lycopene from gac arils using the microwave extraction method. Response surface method was used to find the conditions that optimize the extraction of lycopene from gac arils. The parameters of extraction used in this study were extraction time (120-600 seconds), the solvent to sample ratio (10:1, 20:1, 30:1, 40:1 and 50:1 mL/g) and set microwave power (100-800 watts). The results showed that the microwave extraction condition at the extraction time of 360 seconds, the sample ratio of 30:1 mL/g and the microwave power of 450 watts were suggested since it exhibited the highest value of lycopene content of 9.86 mg/gDW. It was also observed that lycopene contents extracted from gac arils by microwave method were higher than that by the conventional method. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=conventional%20extraction" title="conventional extraction">conventional extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=Gac%20arils" title=" Gac arils"> Gac arils</a>, <a href="https://publications.waset.org/abstracts/search?q=microwave-assisted%20extraction" title=" microwave-assisted extraction"> microwave-assisted extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=Lycopene" title=" Lycopene"> Lycopene</a> </p> <a href="https://publications.waset.org/abstracts/62117/microwave-assisted-extraction-of-lycopene-from-gac-arils-momordica-cochinchinensis-lour-spreng" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/62117.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">390</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4208</span> Solvent extraction of molybdenum (VI) with two organophosphorus reagents TBP and D2EHPA under microwave irradiations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ahmed%20Boucherit">Ahmed Boucherit</a>, <a href="https://publications.waset.org/abstracts/search?q=Hussein%20Khalaf"> Hussein Khalaf</a>, <a href="https://publications.waset.org/abstracts/search?q=Eduardo%20Paredes"> Eduardo Paredes</a>, <a href="https://publications.waset.org/abstracts/search?q=Jos%C3%A9%20Luis%20Todol%C3%AD"> José Luis Todolí</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Solvent extraction studies of molybdenum (VI) with two organophosphorus reagents namely TBP and D2EHPA have been carried out from aqueous acidic solutions of HCl, H2SO4 and H3PO4 under microwave irradiations. The extraction efficiencies of the investigated extractants in the extraction of molybdenum (Vl) were compared. Extraction yield was found unchanged when microwave power varied in the range 20-100 Watts from H2SO4 or H3PO4 but it decreases in the range 20-60 Watts and increases in the range 60-100 Watts when TBP is used for extraction of molybdenum (VI) from 1 M HCl solutions. Extraction yield of molybdenum (VI) was found higher with TBP for HCl molarities greater than 1 M than with D2EHPA for H3PO4 molarities lower than 1 M. Extraction yield increases with HCl molarities in the range 0.50 - 1.80 M but it decreases with the increase in H2SO4 and H3PO4 molarities in the range of 0.05 - 1 M and 0.50 - 1 M, respectively. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=extraction" title="extraction">extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=molybdenum" title=" molybdenum"> molybdenum</a>, <a href="https://publications.waset.org/abstracts/search?q=microwave" title=" microwave"> microwave</a>, <a href="https://publications.waset.org/abstracts/search?q=solvent" title=" solvent"> solvent</a> </p> <a href="https://publications.waset.org/abstracts/22227/solvent-extraction-of-molybdenum-vi-with-two-organophosphorus-reagents-tbp-and-d2ehpa-under-microwave-irradiations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/22227.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">642</span> </span> </div> </div> <ul class="pagination"> <li class="page-item disabled"><span class="page-link">&lsaquo;</span></li> <li class="page-item active"><span class="page-link">1</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20extraction&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20extraction&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20extraction&page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20extraction&page=5">5</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20extraction&page=6">6</a></li> 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