CINXE.COM

<!DOCTYPE html> <html lang="en" dir="ltr"> <head>  <script async src="https://www.googletagmanager.com/gtag/js?id=G-P63WKM1TM1"></script> <script> window.dataLayer = window.dataLayer || []; function gtag(){dataLayer.push(arguments);} gtag('js', new Date()); gtag('config', 'G-P63WKM1TM1'); </script>  <script type="text/javascript" > (function(m,e,t,r,i,k,a){m[i]=m[i]||function(){(m[i].a=m[i].a||[]).push(arguments)}; m[i].l=1*new Date(); for (var j = 0; j < document.scripts.length; j++) {if (document.scripts[j].src === r) { return; }} k=e.createElement(t),a=e.getElementsByTagName(t)[0],k.async=1,k.src=r,a.parentNode.insertBefore(k,a)}) (window, document, "script", "https://mc.yandex.ru/metrika/tag.js", "ym"); ym(55165297, "init", { clickmap:false, trackLinks:true, accurateTrackBounce:true, webvisor:false }); </script> <noscript><div><img src="https://mc.yandex.ru/watch/55165297" style="position:absolute; left:-9999px;" alt="" /></div></noscript>    <title>Search results for: immobilization of fructosyltransferase</title> <meta name="description" content="Search results for: immobilization of fructosyltransferase"> <meta name="keywords" content="immobilization of fructosyltransferase"> <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 navbar-toggler ml-auto" type="button" data-toggle="collapse" data-target="#navbarMenu" aria-controls="navbarMenu" aria-expanded="false" aria-label="Toggle navigation"> <span class="navbar-toggler-icon"></span> </button> <div class="w-100"> <div class="d-none d-lg-flex flex-row-reverse"> <form method="get" action="https://waset.org/search" class="form-inline my-2 my-lg-0"> <input class="form-control mr-sm-2" type="search" placeholder="Search Conferences" value="immobilization of fructosyltransferase" name="q" aria-label="Search"> <button class="btn btn-light my-2 my-sm-0" type="submit"><i class="fas fa-search"></i></button> </form> </div> <div class="collapse navbar-collapse mt-1" id="navbarMenu"> <ul class="navbar-nav ml-auto align-items-center" id="mainNavMenu"> <li class="nav-item"> <a class="nav-link" href="https://waset.org/conferences" title="Conferences in 2024/2025/2026">Conferences</a> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/disciplines" title="Disciplines">Disciplines</a> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/committees" rel="nofollow">Committees</a> </li> <li class="nav-item dropdown"> <a class="nav-link dropdown-toggle" href="#" id="navbarDropdownPublications" role="button" data-toggle="dropdown" aria-haspopup="true" aria-expanded="false"> Publications </a> <div class="dropdown-menu" aria-labelledby="navbarDropdownPublications"> <a class="dropdown-item" href="https://publications.waset.org/abstracts">Abstracts</a> <a class="dropdown-item" href="https://publications.waset.org">Periodicals</a> <a class="dropdown-item" href="https://publications.waset.org/archive">Archive</a> </div> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/page/support" title="Support">Support</a> </li> </ul> </div> </div> </nav> </div> </header> <main> <div class="container mt-4"> <div class="row"> <div class="col-md-9 mx-auto"> <form method="get" 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="immobilization of fructosyltransferase"> <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> 163</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: immobilization of fructosyltransferase</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">163</span> Selective Immobilization of Fructosyltransferase onto Glutaraldehyde Modified Support and Its Application in the Production of Fructo-Oligosaccharides</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Milica%20B.%20Veljkovi%C4%87">Milica B. Veljković</a>, <a href="https://publications.waset.org/abstracts/search?q=Milica%20B.%20Simovi%C4%87"> Milica B. Simović</a>, <a href="https://publications.waset.org/abstracts/search?q=Marija%20M.%20%C4%86orovi%C4%87"> Marija M. Ćorović</a>, <a href="https://publications.waset.org/abstracts/search?q=Ana%20D.%20Milivojevi%C4%87"> Ana D. Milivojević</a>, <a href="https://publications.waset.org/abstracts/search?q=Anja%20I.%20Petrov"> Anja I. Petrov</a>, <a href="https://publications.waset.org/abstracts/search?q=Katarina%20M.%20Banjanac"> Katarina M. Banjanac</a>, <a href="https://publications.waset.org/abstracts/search?q=Dejan%20I.%20Bezbradica"> Dejan I. Bezbradica</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In recent decades, the scientific community has recognized the growing importance of prebiotics, and therefore, numerous studies are focused on their economic production due to their low presence in natural resources. It has been confirmed that prebiotics is a source of energy for probiotics in the gastrointestinal tract (GIT) and enable their proliferation, consequently leading to the normal functioning of the intestinal microbiota. Also, products of their fermentation are short-chain fatty acids (SCFA), which play a key role in maintaining and improving the health not only of the GIT but also of the whole organism. Among several confirmed prebiotics, fructooligosaccharides (FOS) are considered interesting candidates for use in a wide range of products in the food industry. They are characterized as low-calorie and non-cariogenic substances that represent an adequate sugar substitute and can be considered suitable for use in products intended for diabetics. The subject of this research will be the production of FOS by transforming sucrose using a fructosyltransferase (FTase) present in commercial preparation Pectinex® Ultra SP-L, with special emphasis on the development of adequate FTase immobilization method that would enable selective isolation of the enzyme responsible for the synthesis of FOS from the complex enzymatic mixture. This would lead to considerable enzyme purification and allow its direct incorporation into different sucrose-based products without the fear that the action of the other hydrolytic enzymes may adversely affect the products' functional characteristics. Accordingly, the possibility of selective immobilization of the enzyme using support with primary amino groups, Purolite® A109, which was previously activated and modified using glutaraldehyde (GA), was investigated. In the initial phase of the research, the effects of individual immobilization parameters such as pH, enzyme concentration, and immobilization time were investigated to optimize the process using support chemically activated with 15% and 0.5% GA to form dimers and monomers, respectively. It was determined that highly active immobilized preparations (371.8 IU/g of support - dimer and 213.8 IU/g of support – monomer) were achieved under acidic conditions (pH 4) provided that an enzyme concentration was 50 mg/g of support after 7 h and 3 h, respectively. Bearing in mind the obtained results of the expressed activity, it is noticeable that the formation of dimers showed higher reactivity compared to the form of monomers. Also, in the case of support modification using 15% GA, the value of the ratio of FTase and pectinase (as dominant enzyme mixture component) activity immobilization yields was 16.45, indicating the high feasibility of selective immobilization of FTase on modified polystyrene resin. After obtaining immobilized preparations of satisfactory features, they were tested in a reaction of FOS synthesis under determined optimal conditions. The maximum FOS yields of approximately 50% of total carbohydrates in the reaction mixture were recorded after 21 h. Finally, it can be concluded that the examined immobilization method yielded highly active, stable and, more importantly, refined enzyme preparation that can be further utilized on a larger scale for the development of continual processes for FOS synthesis, as well as for modification of different sucrose-based mediums. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chemical%20modification" title="chemical modification">chemical modification</a>, <a href="https://publications.waset.org/abstracts/search?q=fructooligosaccharides" title=" fructooligosaccharides"> fructooligosaccharides</a>, <a href="https://publications.waset.org/abstracts/search?q=glutaraldehyde" title=" glutaraldehyde"> glutaraldehyde</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization%20of%20fructosyltransferase" title=" immobilization of fructosyltransferase"> immobilization of fructosyltransferase</a> </p> <a href="https://publications.waset.org/abstracts/145471/selective-immobilization-of-fructosyltransferase-onto-glutaraldehyde-modified-support-and-its-application-in-the-production-of-fructo-oligosaccharides" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/145471.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">186</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">162</span> Immobilization of Lipase Enzyme by Low Cost Material: A Statistical Approach</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Md.%20Z.%20Alam">Md. Z. Alam</a>, <a href="https://publications.waset.org/abstracts/search?q=Devi%20R.%20Asih"> Devi R. Asih</a>, <a href="https://publications.waset.org/abstracts/search?q=Md.%20N.%20Salleh"> Md. N. Salleh</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Immobilization of lipase enzyme produced from palm oil mill effluent (POME) by the activated carbon (AC) among the low cost support materials was optimized. The results indicated that immobilization of 94% was achieved by AC as the most suitable support material. A sequential optimization strategy based on a statistical experimental design, including one-factor-at-a-time (OFAT) method was used to determine the equilibrium time. Three components influencing lipase immobilization were optimized by the response surface methodology (RSM) based on the face-centered central composite design (FCCCD). On the statistical analysis of the results, the optimum enzyme concentration loading, agitation rate and carbon active dosage were found to be 30 U/ml, 300 rpm and 8 g/L respectively, with a maximum immobilization activity of 3732.9 U/g-AC after 2 hrs of immobilization. Analysis of variance (ANOVA) showed a high regression coefficient (R2) of 0.999, which indicated a satisfactory fit of the model with the experimental data. The parameters were statistically significant at p<0.05. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=activated%20carbon" title="activated carbon">activated carbon</a>, <a href="https://publications.waset.org/abstracts/search?q=POME%20based%20lipase" title=" POME based lipase"> POME based lipase</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=adsorption" title=" adsorption"> adsorption</a> </p> <a href="https://publications.waset.org/abstracts/9053/immobilization-of-lipase-enzyme-by-low-cost-material-a-statistical-approach" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/9053.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">243</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">161</span> Medium Composition for the Laboratory Production of Enzyme Fructosyltransferase (FTase)</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=O.%20R.%20Raimi">O. R. Raimi</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Lateef"> A. Lateef</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Inoculum developments of A. niger were used for inoculation of medium for submerged fermentation and solid state fermentation. The filtrate obtained were used as sources of the extra-cellular enzymes. The FTase activities and the course of pH in submerged fermentation ranged from 7.53-24.42µ/ml and 4.4-4.8 respectively. The maximum FTase activity was obtained at 48 hours fermentation. In solid state fermentation, FTase activities ranged from 2.41-27.77µ/ml. Using ripe plantain peel and kola nut pod respectively. Both substrates supported the growth of the fungus, producing profuse growth during fermentation. In the control experiment (using kolanut pod) that lack supplementation, appreciable FTase activity of 16.92µ/ml was obtained. The optimum temperature range was 600C. it was also active at broad pH range of 1-9 with optimum obtain at pH of 5.0. FTase was stable within the range of investigated pH showing more than 60% activities. FTase can be used in the production of fructooligosaccharide, a functional food. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Aspergillus%20niger" title="Aspergillus niger">Aspergillus niger</a>, <a href="https://publications.waset.org/abstracts/search?q=solid%20state%20fermentation" title=" solid state fermentation"> solid state fermentation</a>, <a href="https://publications.waset.org/abstracts/search?q=kola%20nut%20pods" title=" kola nut pods"> kola nut pods</a>, <a href="https://publications.waset.org/abstracts/search?q=Fructosyltransferase%20%28FTase%29" title=" Fructosyltransferase (FTase)"> Fructosyltransferase (FTase)</a> </p> <a href="https://publications.waset.org/abstracts/2063/medium-composition-for-the-laboratory-production-of-enzyme-fructosyltransferase-ftase" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2063.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">457</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">160</span> Pectin Degrading Enzyme: Entrapment of Pectinase Using Different Synthetic and Non-Synthetic Polymers for Continuous Degradation of Pectin Polymer </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Haneef%20Ur%20Rehman">Haneef Ur Rehman</a>, <a href="https://publications.waset.org/abstracts/search?q=Afsheen%20Aman"> Afsheen Aman</a>, <a href="https://publications.waset.org/abstracts/search?q=Abdul%20Hameed%20Baloch"> Abdul Hameed Baloch</a>, <a href="https://publications.waset.org/abstracts/search?q=Shah%20Ali%20Ul%20Qader"> Shah Ali Ul Qader</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Pectinase is a heterogeneous group of enzymes that catalyze the hydrolysis of pectin substances and widely has been used in food and textile industries. In current study, pectinase from B. licheniformis KIBGE-IB21 was immobilized within different polymers (calcium alginate beads, polyacrylamide gel and agar-agar matrix) to enhance its catalytic properties. Polyacrylamide gel was found to be most promising one and gave maximum (89%) immobilization yield. While less immobilization yield was observed in case of calcium alginate beads that only retained 46 % activity. The reaction time for maximum pectinolytic activity was increased from 5.0 to 10 minutes after immobilization. The temperature of pectinase for maximum enzyme activity was increased from 45 °C to 50 °C and 55 °C when it was immobilized within agar-agar and calcium alginate beads, respectively. The optimum pH of pectinase didn’t alter when it was immobilized within polyacrylamide gel and calcium alginate beads, but in case of agar-agar it was changed from pH 10 to pH 9.0. Thermal stability of pectinase was improved after immobilization and immobilized pectinase showed higher toleration against different temperatures as compared to free enzyme. It can be concluded that the entrapment is a simple, single step and promising procedure to immobilized pectinase within different synthetic and non-synthetic polymers and enhanced its catalytic properties. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=pectinase" title="pectinase">pectinase</a>, <a href="https://publications.waset.org/abstracts/search?q=characterization%20immobilization" title=" characterization immobilization"> characterization immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=polyacrylamide" title=" polyacrylamide"> polyacrylamide</a>, <a href="https://publications.waset.org/abstracts/search?q=agar-agar" title=" agar-agar"> agar-agar</a>, <a href="https://publications.waset.org/abstracts/search?q=calcium%20alginate%20beads" title=" calcium alginate beads"> calcium alginate beads</a> </p> <a href="https://publications.waset.org/abstracts/21905/pectin-degrading-enzyme-entrapment-of-pectinase-using-different-synthetic-and-non-synthetic-polymers-for-continuous-degradation-of-pectin-polymer" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/21905.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">606</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">159</span> Magnetic Silica Nanoparticles as Viable Support for the Immobilization of Oxidative Enzymes</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Y.%20Moldes-Diz">Y. Moldes-Diz</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Gamallo"> M. Gamallo</a>, <a href="https://publications.waset.org/abstracts/search?q=G.%20Eibes"> G. Eibes</a>, <a href="https://publications.waset.org/abstracts/search?q=C.%20Vazquez-Vazquez"> C. Vazquez-Vazquez</a>, <a href="https://publications.waset.org/abstracts/search?q=G.%20Feijoo"> G. Feijoo</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20M.%20Lema"> J. M. Lema</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20T.%20Moreira"> M. T. Moreira</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Laccases (benzenediol oxygen oxidoreductases, EC 1.10.3.2) are excellent biocatalysts for biotechnological and environmental applications because of their high activity, selectivity, and specificity. Specifically, these characteristics allow them to perform the oxidation of recalcitrant compounds with simple requirements for the catalysis (presence of molecular oxygen). Nevertheless, the low stability under unfavorable conditions (pH, inactivating agents or temperature) and high production costs still limits their use for practical applications. Immobilization of enzymes has proven particularly valuable to avoid some of the aforementioned drawbacks. Magnetic nanoparticles (MNPs) have received increasing attention as carriers for enzyme immobilization since they can potentially provide an easy recovery of the biocatalyst from the reaction medium under an external magnetic field. In the present work, silica-coated magnetic nanoparticles (Fe3O4@SiO2) were prepared, characterized and used for laccase immobilization by covalent binding. The synthesis of Fe3O4@SiO2 was performed in a two-step procedure: co-precipitation and reverse microemulsion. The influence of immobilization conditions: concentrations of the functionalization agent (3-aminopropyl-triethoxy-silane) and the cross-linker (glutaraldehyde) as well as the influence of pH, T or inactivating agents were evaluated. In general, immobilized laccase showed superior stability compared to that of free enzyme. The reusability of the biocatalyst was demonstrated in successive batch reactions, where enzyme activity was maintained above 65% after 8 cycles of oxidation of the substrate 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=silica-coated%20magnetic%20nanoparticles" title="silica-coated magnetic nanoparticles">silica-coated magnetic nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=laccase" title=" laccase"> laccase</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=regeneration" title=" regeneration"> regeneration</a> </p> <a href="https://publications.waset.org/abstracts/55780/magnetic-silica-nanoparticles-as-viable-support-for-the-immobilization-of-oxidative-enzymes" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/55780.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">158</span> Immobilization of Enzymes and Proteins on Epoxy-Activated Supports</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ehsan%20Khorshidian">Ehsan Khorshidian</a>, <a href="https://publications.waset.org/abstracts/search?q=Afshin%20Farahbakhsh"> Afshin Farahbakhsh</a>, <a href="https://publications.waset.org/abstracts/search?q=Sina%20Aghili"> Sina Aghili</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Enzymes are promising biocatalysts for many organic reactions. They have excellent features like high activity, specificity and selectivity, and can catalyze under mild and environment friendly conditions. Epoxy-activated supports are almost-ideal ones to perform very easy immobilization of proteins and enzymes at both laboratory and industrial scale. The activated epoxy supports (chitosan/alginate, Eupergit C) may be very suitable to achieve the multipoint covalent attachment of proteins and enzymes, therefore, to stabilize their three-dimensional structure. The enzyme is firstly covalently immobilized under conditions pH 7.0 and 10.0. The remaining groups of the support are blocked to stop additional interaction between the enzyme and support by mercaptoethanol or Triton X-100. The results show support allowed obtaining biocatalysts with high immobilized protein amount and hydrolytic activity. The immobilization of lipases on epoxy support may be considered as attractive tool for obtaining highly active biocatalysts to be used in both aqueous and anhydrous aqueous media. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=immobilization%20of%20enzymes" title="immobilization of enzymes">immobilization of enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=epoxy%20supports" title=" epoxy supports"> epoxy supports</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20multipoint%20covalent%20attachment" title=" enzyme multipoint covalent attachment"> enzyme multipoint covalent attachment</a>, <a href="https://publications.waset.org/abstracts/search?q=microbial%20lipases" title=" microbial lipases"> microbial lipases</a> </p> <a href="https://publications.waset.org/abstracts/9260/immobilization-of-enzymes-and-proteins-on-epoxy-activated-supports" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/9260.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">388</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">157</span> Indicator-Immobilized, Cellulose Based Optical Sensing Membrane for the Detection of Heavy Metal Ions</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Nisha%20Dhariwal">Nisha Dhariwal</a>, <a href="https://publications.waset.org/abstracts/search?q=Anupama%20Sharma"> Anupama Sharma</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The synthesis of cellulose nanofibrils quaternized with 3‐chloro‐2‐hydroxypropyltrimethylammonium chloride (CHPTAC) in NaOH/urea aqueous solution has been reported. Xylenol Orange (XO) has been used as an indicator for selective detection of Sn (II) ions, by its immobilization on quaternized cellulose membrane. The effects of pH, reagent concentration and reaction time on the immobilization of XO have also been studied. The linear response, limit of detection, and interference of other metal ions have also been studied and no significant interference has been observed. The optical chemical sensor displayed good durability and short response time with negligible leaching of the reagent. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cellulose" title="cellulose">cellulose</a>, <a href="https://publications.waset.org/abstracts/search?q=chemical%20sensor" title=" chemical sensor"> chemical sensor</a>, <a href="https://publications.waset.org/abstracts/search?q=heavy%20metal%20ions" title=" heavy metal ions"> heavy metal ions</a>, <a href="https://publications.waset.org/abstracts/search?q=indicator%20immobilization" title=" indicator immobilization"> indicator immobilization</a> </p> <a href="https://publications.waset.org/abstracts/43826/indicator-immobilized-cellulose-based-optical-sensing-membrane-for-the-detection-of-heavy-metal-ions" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/43826.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">301</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">156</span> Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-Linked Enzyme Aggregates</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=S.%20Md.%20Shaarani">S. Md. Shaarani</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Md.%20Jahim"> J. Md. Jahim</a>, <a href="https://publications.waset.org/abstracts/search?q=R.%20A.%20Rahman"> R. A. Rahman</a>, <a href="https://publications.waset.org/abstracts/search?q=R.%20Md.%20Illias"> R. Md. Illias</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Modern developments in biotechnology have paved the way for extensive use of biocatalysis in industries. Although it offers immense potential, industrial application is usually hampered by lack of operational stability, difficulty in recovery as well as limited re-use of the enzyme. These drawbacks, however, can be overcome by immobilization. Cross-linked enzyme aggregates (CLEAs), a versatile carrier-free immobilization technique is one that is currently capturing global interest. This approach involves precipitating soluble enzyme with an appropriate precipitant and subsequent crosslinking by a crosslinking reagent. Without ineffective carriers, CLEAs offer high enzymatic activity, stability and reduced production cost. This study demonstrated successful CLEA synthesis of recombinant xylanase from Trichoderma reesei using ethanol as aggregating agent and glutaraldehyde (2% (v/v); 100 mM) as crosslinker. Effects of additives including proteic feeder such as bovine serum albumin (BSA) and poly-L-Lysine were investigated to reveal its significance in enhancing the performance of enzyme. Addition of 0.1 mg BSA/U xylanase showed considerable increment in CLEA development with approximately 50% retained activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cross-linked" title="cross-linked">cross-linked</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=recombinant" title=" recombinant"> recombinant</a>, <a href="https://publications.waset.org/abstracts/search?q=xylanase" title=" xylanase"> xylanase</a> </p> <a href="https://publications.waset.org/abstracts/9446/immobilization-strategy-of-recombinant-xylanase-from-trichoderma-reesei-by-cross-linked-enzyme-aggregates" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/9446.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">358</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">155</span> Fluoride Immobilization in Plaster Board Waste: A Safety Measure to Prevent Soil and Water Pollution</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Venkataraman%20Sivasankar">Venkataraman Sivasankar</a>, <a href="https://publications.waset.org/abstracts/search?q=Kiyoshi%20Omine"> Kiyoshi Omine</a>, <a href="https://publications.waset.org/abstracts/search?q=Hideaki%20Sano"> Hideaki Sano</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The leaching of fluoride from Plaster Board Waste (PBW) is quite feasible in soil and water environments. The Ministry of Environment, Japan recommended the standard limit of 0.8 mgL⁻¹ or less for fluoride. Although the utilization of PBW as a substitute for cement is rather meritorious, its fluoride leaching behavior deteriorates the quality of soil and water and therefore envisaged as a demerit. In view of this fluoride leaching problem, the present research is focused on immobilizing fluoride in PBW. The immobilization experiments were conducted with four chemical systems operated by DAHP (diammonium hydrogen phosphate) and phosphoric acid carbonization of bamboo mass coupled with certain inorganic reactions using reagents such as calcium hydroxide, sodium hydroxide, and aqueous ammonia. The fluoride immobilization was determined after shaking the reactor contents including the plaster board waste for 24 h at 25˚C. In the DAHP system, the immobilization of fluoride was evident from the leaching of fluoride in the range 0.071-0.12 mgL⁻¹, 0.026-0.14 mgL⁻¹ and 0.068-0.12 mgL⁻¹ for the reaction temperatures at 30˚C, 50˚C, and 90˚C, respectively, with final pH of 6.8. The other chemical systems designated as PACCa, PACAm, and PACNa could immobilize fluoride in PBW, and the resulting solution was analyzed with the fluoride less than the Japanese environmental standard of 0.8 mgL⁻¹. In the case of PACAm and PACCa systems, the calcium concentration was found undetectable and witnessed the formation of phosphate compounds. The immobilization of fluoride was found inversely proportional to the increase in the volume of leaching solvent and dose of PBW. Characterization studies of PBW and the solid after fluoride immobilization was done using FTIR (Fourier transform infrared spectroscopy), Raman spectroscopy, FE-SEM ( Field Emission Scanning Electron Microscopy) with EDAX (Energy Dispersive Spectroscopy), XRD (X-ray diffraction), and XPS (X-ray photoelectron spectroscopy). The results revealed the formation of new calcium phosphate compounds such as apatite, monetite, and hydroxylapatite. The participation of such new compounds in fluoride immobilization seems indispensable through the exchange mechanism of hydroxyl and fluoride groups. Acknowledgment: First author thanks to Japanese Society for the Promotion of Science (JSPS) for the award of the fellowship (ID No. 16544). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=characterization" title="characterization">characterization</a>, <a href="https://publications.waset.org/abstracts/search?q=fluoride" title=" fluoride"> fluoride</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=plaster%20board%20waste" title=" plaster board waste"> plaster board waste</a> </p> <a href="https://publications.waset.org/abstracts/84240/fluoride-immobilization-in-plaster-board-waste-a-safety-measure-to-prevent-soil-and-water-pollution" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/84240.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">157</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">154</span> High Catalytic Activity and Stability of Ginger Peroxidase Immobilized on Amino Functionalized Silica Coated Titanium Dioxide Nanocomposite: A Promising Tool for Bioremediation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Misha%20Ali">Misha Ali</a>, <a href="https://publications.waset.org/abstracts/search?q=Qayyum%20Husain"> Qayyum Husain</a>, <a href="https://publications.waset.org/abstracts/search?q=Nida%20Alam"> Nida Alam</a>, <a href="https://publications.waset.org/abstracts/search?q=Masood%20%20Ahmad"> Masood Ahmad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Improving the activity and stability of the enzyme is an important aspect in bioremediation processes. Immobilization of enzyme is an efficient approach to amend the properties of biocatalyst required during wastewater treatment. The present study was done to immobilize partially purified ginger peroxidase on amino functionalized silica coated titanium dioxide nanocomposite. Interestingly there was an enhancement in enzyme activity after immobilization on nanosupport which was evident from effectiveness factor (η) value of 1.76. Immobilized enzyme was characterized by transmission electron microscopy, scanning electron microscopy and Fourier transform infrared spectroscopy. Immobilized peroxidase exhibited higher activity in a broad range of pH and temperature as compared to free enzyme. Also, the thermostability of peroxidase was strikingly improved upon immobilization. After six repeated uses, the immobilized peroxidase retained around 62% of its dye decolorization activity. There was a 4 fold increase in Vmax of immobilized peroxidase as compared to free enzyme. Circular dichroism spectroscopy demonstrated conformational changes in the secondary structure of enzyme, a possible reason for the enhanced enzyme activity after immobilization. Immobilized peroxidase was highly efficient in the removal of acid yellow 42 dye in a stirred batch process. Our study shows that this bio-remediating system has remarkable potential for treatment of aromatic pollutants present in wastewater. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=acid%20yellow%2042" title="acid yellow 42">acid yellow 42</a>, <a href="https://publications.waset.org/abstracts/search?q=decolorization" title=" decolorization"> decolorization</a>, <a href="https://publications.waset.org/abstracts/search?q=ginger%20peroxidase" title=" ginger peroxidase"> ginger peroxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a> </p> <a href="https://publications.waset.org/abstracts/57680/high-catalytic-activity-and-stability-of-ginger-peroxidase-immobilized-on-amino-functionalized-silica-coated-titanium-dioxide-nanocomposite-a-promising-tool-for-bioremediation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/57680.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">249</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">153</span> Preparation of Low-Molecular-Weight 6-Amino-6-Deoxychitosan (LM6A6DC) for Immobilization of Growth Factor</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Koo-Yeon%20Kim">Koo-Yeon Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Eun-Hye%20Kim"> Eun-Hye Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Tae-Il%20Son"> Tae-Il Son</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Epidermal Growth Factor (EGF, Mw=6,045) has been reported to have high efficiency of wound repair and anti-wrinkle effect. However, the half-life of EGF in the body is too short to exert the biological activity effectively when applied in free form. Growth Factors can be stabilized by immobilization with carbohydrates from thermal and proteolytic degradation. Low molecular weight chitosan (LMCS) and its derivate prepared by hydrogen peroxide has high solubility. LM6A6DC was successfully prepared as a reactive carbohydrate for the stabilization of EGF by the reactions of LMCS with alkalization, tosylation, azidation and reduction. The structure of LM6A6DC was confirmed by FT-IR, 1H NMR and elementary analysis. For enhancing the stability of free EGF, EGF was attached with LM6A6DC by using water-soluble carbodiimide. EGF-LM6A6DC conjugates did not show any cytotoxicity on the Normal Human Dermal Fibroblast(NHDF) 3T3 proliferation at least under 100 ㎍/㎖. In the result, it was considered that LM6A6DC is suitable to immobilize of growth factor. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=epidermal%20growth%20factor%20%28EGF%29" title="epidermal growth factor (EGF)">epidermal growth factor (EGF)</a>, <a href="https://publications.waset.org/abstracts/search?q=low-molecular-weight%20chitosan" title=" low-molecular-weight chitosan"> low-molecular-weight chitosan</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a> </p> <a href="https://publications.waset.org/abstracts/21422/preparation-of-low-molecular-weight-6-amino-6-deoxychitosan-lm6a6dc-for-immobilization-of-growth-factor" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/21422.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">473</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">152</span> Inclusion Body Refolding at High Concentration for Large-Scale Applications</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=J.%20Gabrielczyk">J. Gabrielczyk</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Kluitmann"> J. Kluitmann</a>, <a href="https://publications.waset.org/abstracts/search?q=T.%20Dammeyer"> T. Dammeyer</a>, <a href="https://publications.waset.org/abstracts/search?q=H.%20J.%20J%C3%B6rdening"> H. J. Jördening</a> </p> <p class="card-text"><strong>Abstract:</strong></p> High-level expression of proteins in bacteria often causes production of insoluble protein aggregates, called inclusion bodies (IB). They contain mainly one type of protein and offer an easy and efficient way to get purified protein. On the other hand, proteins in IB are normally devoid of function and therefore need a special treatment to become active. Most refolding techniques aim at diluting the solubilizing chaotropic agents. Unfortunately, optimal refolding conditions have to be found empirically for every protein. For large-scale applications, a simple refolding process with high yields and high final enzyme concentrations is still missing. The constructed plasmid pASK-IBA63b containing the sequence of fructosyltransferase (FTF, EC 2.4.1.162) from Bacillus subtilis NCIMB 11871 was transformed into E. coli BL21 (DE3) Rosetta. The bacterium was cultivated in a fed-batch bioreactor. The produced FTF was obtained mainly as IB. For refolding experiments, five different amounts of IBs were solubilized in urea buffer with protein concentration of 0.2-8.5 g/L. Solubilizates were refolded with batch or continuous dialysis. The refolding yield was determined by measuring the protein concentration of the clear supernatant before and after the dialysis. Particle size was measured by dynamic light scattering. We tested the solubilization properties of fructosyltransferase IBs. The particle size measurements revealed that the solubilization of the aggregates is achieved at urea concentration of 5M or higher and confirmed by absorption spectroscopy. All results confirm previous investigations that refolding yields are dependent upon initial protein concentration. In batch dialysis, the yields dropped from 67% to 12% and 72% to 19% for continuous dialysis, in relation to initial concentrations from 0.2 to 8.5 g/L. Often used additives such as sucrose and glycerol had no effect on refolding yields. Buffer screening indicated a significant increase in activity but also temperature stability of FTF with citrate/phosphate buffer. By adding citrate to the dialysis buffer, we were able to increase the refolding yields to 82-47% in batch and 90-74% in the continuous process. Further experiments showed that in general, higher ionic strength of buffers had major impact on refolding yields; doubling the buffer concentration increased the yields up to threefold. Finally, we achieved corresponding high refolding yields by reducing the chamber volume by 75% and the amount of buffer needed. The refolded enzyme had an optimal activity of 12.5±0.3 x104 units/g. However, detailed experiments with native FTF revealed a reaggregation of the molecules and loss in specific activity depending on the enzyme concentration and particle size. For that reason, we actually focus on developing a process of simultaneous enzyme refolding and immobilization. The results of this study show a new approach in finding optimal refolding conditions for inclusion bodies at high concentrations. Straightforward buffer screening and increase of the ionic strength can optimize the refolding yield of the target protein by 400%. Gentle removal of chaotrope with continuous dialysis increases the yields by an additional 65%, independent of the refolding buffer applied. In general time is the crucial parameter for successful refolding of solubilized proteins. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=dialysis" title="dialysis">dialysis</a>, <a href="https://publications.waset.org/abstracts/search?q=inclusion%20body" title=" inclusion body"> inclusion body</a>, <a href="https://publications.waset.org/abstracts/search?q=refolding" title=" refolding"> refolding</a>, <a href="https://publications.waset.org/abstracts/search?q=solubilization" title=" solubilization"> solubilization</a> </p> <a href="https://publications.waset.org/abstracts/36720/inclusion-body-refolding-at-high-concentration-for-large-scale-applications" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/36720.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">294</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">151</span> Enzyme Immobilization: A Strategy to Overcome Enzyme Limitations and Expand Their Applications</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Charline%20Monnier">Charline Monnier</a>, <a href="https://publications.waset.org/abstracts/search?q=Rudolf%20Andrys"> Rudolf Andrys</a>, <a href="https://publications.waset.org/abstracts/search?q=Irene%20Castellino"> Irene Castellino</a>, <a href="https://publications.waset.org/abstracts/search?q=Lucie%20Zemanova"> Lucie Zemanova</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Due to their inherent sustainability and compatibility with green chemistry principles, enzymes are attracting increasing attention for various applications like bioremediation or biocatalysis. These natural catalysts boast remarkable substrate specificity and operate under mild biological conditions. However, their intrinsic limitations, such as instability at high temperatures or in organic solvents, impede their wider applicability. Enzyme immobilization on supportive matrices emerges as a promising strategy to address these challenges. This approach not only facilitates enzyme reusability but also offers the potential to modulate their stability, activity, and selectivity. The present study investigates the immobilization and application of two distinct groups of hydrolases on supportive matrices: PETases, naturally capable of PolyEthylene Terephthalate (PET) degradation, and cholinesterases (ChEs), key enzymes in neurotransmitter regulation. All tested enzymes will be immobilized on porous and non-porous particles using both covalent and non-covalent methods. Additionally, the stability of PETases and cholinesterases will be explored, followed by exposure to denaturing conditions to assess their resilience under harsh conditions. Furthermore, due to the exceptional catalytic efficiency and selectivity, their biocatalytic efficiency will be tested using xenobiotic substrates, aiming to establish them as replacements for conventional chemical catalysts in environmentally friendly processes. By exploiting the power of enzyme immobilization, this research strives to unlock the full potential of these biocatalysts for sustainable and efficient technological advancements. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biocatalysis" title="biocatalysis">biocatalysis</a>, <a href="https://publications.waset.org/abstracts/search?q=bioremediation" title=" bioremediation"> bioremediation</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20efficiency" title=" enzyme efficiency"> enzyme efficiency</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20immobilization" title=" enzyme immobilization"> enzyme immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=green%20chemistry" title=" green chemistry"> green chemistry</a> </p> <a href="https://publications.waset.org/abstracts/182976/enzyme-immobilization-a-strategy-to-overcome-enzyme-limitations-and-expand-their-applications" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/182976.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">57</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">150</span> Immobilization of β-Galactosidase from Kluyveromyces Lactis on Polyethylenimine-Agarose for Production of Lactulose</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Carlos%20A.%20C.%20G.%20Neto">Carlos A. C. G. Neto</a>, <a href="https://publications.waset.org/abstracts/search?q=Natan%20C.%20G.%20Silva"> Natan C. G. Silva</a>, <a href="https://publications.waset.org/abstracts/search?q=Thais%20O.%20Costa"> Thais O. Costa</a>, <a href="https://publications.waset.org/abstracts/search?q=Luciana%20R.%20B.%20%20Goncalves"> Luciana R. B. Goncalves</a>, <a href="https://publications.waset.org/abstracts/search?q=Maria%20v.%20P.%20%20Rocha"> Maria v. P. Rocha</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Galactosidases are enzymes responsible for catalyzing lactose hydrolysis reactions and also favoring transgalactosylation reactions for the production of prebiotics, among which lactulose stands out. These enzymes, when immobilized, can have some enzymatic characteristics substantially improved, and the coating of supports with multifunctional polymers in immobilization processes is a promising alternative in order to extend the useful life of the biocatalysts, for example, the coating with polyethyleneimine (PEI). PEI is a flexible polymer that suits the structure of the enzyme, giving greater stability, especially for multimeric enzymes such as β-galactosidases and also protects it from environmental variations, for example, pH and temperature. In addition, it can substantially improve the immobilization parameters and also the efficiency of enzymatic reactions. In this context, the aim of the present work was first to develop biocatalysts of β-galactosidase from Kluyveromyces lactis immobilized on PEI coated agarose, determining the immobilization parameters, its operational and thermal stability, and then to apply it in the hydrolysis of lactose and synthesis of lactulose, using whey as a substrate. This immobilization strategy was chosen in order to improve the catalytic efficiency of the enzyme in the transgalactosylation reaction for the production of prebiotics, and there are few studies with β-galactosidase from this strain. The immobilization of β-galactosidase in agarose previously functionalized with 48% (w/v) glycidol and then coated with 10% (w/v) PEI solution was evaluated using an enzymatic load of 10 mg/g of protein. Subsequently, the hydrolysis and transgalactosylation reactions were conducted at 50 °C, 120 RPM for 20 minutes, using whey (66.7 g/L of lactose) supplemented with 133.3 g/L fructose at a ratio of 1:2 (lactose/fructose). Operational stability studies were performed in the same conditions for 10 cycles. Thermal stabilities of biocatalysts were conducted at 50 ºC in 50 mM phosphate buffer, pH 6.6, with 0.1 mM MnCl2. The biocatalysts whose supports were coated were named AGA_GLY_PEI_GAL, and those that were not coated were named AGA_GLY_GAL. The coating of the support with PEI considerably improved immobilization yield (2.6-fold), the biocatalyst activity (1.4-fold), and efficiency (2.2-fold). The biocatalyst AGA_GLY_PEI_GAL was better than AGA_GLY_GAL in hydrolysis and transgalactosylation reactions, converting 88.92% of lactose at 5 min of reaction and obtaining a residual concentration of 5.24 g/L. Besides that, it was produced 13.90 g/L lactulose in the same time interval. AGA_GLY_PEI_GAL biocatalyst was stable during the 10 cycles evaluated, converting approximately 80% of lactose and producing 10.95 g/L of lactulose even after the tenth cycle. However, the thermal stability of AGA_GLY_GAL biocatalyst was superior, with a half-life time 5 times higher, probably because the enzyme was immobilized by covalent bonding, which is stronger than adsorption (AGA_GLY_PEI_GAL). Therefore, the strategy of coating the supports with PEI has proven to be effective for the immobilization of β-galactosidase from K. lactis, considerably improving the immobilization parameters, as well as the enzyme, catalyzed reactions. In addition, the use of whey as a raw material for lactulose production has proved to be an industrially advantageous alternative. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=%CE%B2-galactosidase" title="β-galactosidase">β-galactosidase</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=lactulose" title=" lactulose"> lactulose</a>, <a href="https://publications.waset.org/abstracts/search?q=polyethylenimine" title=" polyethylenimine"> polyethylenimine</a>, <a href="https://publications.waset.org/abstracts/search?q=whey" title=" whey"> whey</a> </p> <a href="https://publications.waset.org/abstracts/120441/immobilization-of-v-galactosidase-from-kluyveromyces-lactis-on-polyethylenimine-agarose-for-production-of-lactulose" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/120441.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">119</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">149</span> Co-Immobilization of Palladium Nanoparticles and Polyoxometalate into the Cavities of the Mesocellular Foams: A Biomimetic Cooperative Catalytic System for Aerobic Oxidation of Alcohols under Green Conditions</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Saeed%20Chehri">Saeed Chehri</a>, <a href="https://publications.waset.org/abstracts/search?q=Sirvan%20Moradi"> Sirvan Moradi</a>, <a href="https://publications.waset.org/abstracts/search?q=Amin%20Rostami"> Amin Rostami</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cooperative catalyst systems have been developed as highly promising sustainable alternatives to traditional catalysts. In these catalysts, two or more catalytic centers cooperate to reduce the energy of chemical transformations. In nature, such systems are abundantly seen in metalloenzymes that use metal and an organic cofactor. We have designed a reusable cooperative catalyst oxidation system consisting of palladium nanoparticles and polyoxometalate. This biomimetic cooperative catalytic system was synthesized by the stepwise immobilization of palladium nanoparticlesandpolyoxometalateinto the same cavity of siliceous mesocellularfoams (Pd-POM@MCF)and wascharacterizedby SEM, EDX, FT-IR, TGAand ICP techniques. POM-Pd@MCF/HQexhibits high activity toward aerobic oxidation of alcohols to the corresponding carbonyl compoundsin water solvent at room temperature. The major novelties and advantages of this oxidation method are as follows: (i) this is the first report of the co-immobilization of polyoxometalateand palladium for use as a robust and highlyefficient heterogeneouscooperative oxidative nanocatalyst system for aerobic oxidation of alcohols, (ii) oxidation of alcoholswere performed using an ideal oxidant with good to high yields in a green solvent at ambient temperature and (iii) the immobilization of the oxygen-activating catalyst(polyoxometalate) and oxidizing catalyst (Pd) onto MCF provide practical cooperative catalyst the system that can be reused several times without a significant loss of activity (vi) the methodsconform to several of the guiding principles of green chemistry. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=palladium%20nanoparticles" title="palladium nanoparticles">palladium nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=polyoxometalate" title=" polyoxometalate"> polyoxometalate</a>, <a href="https://publications.waset.org/abstracts/search?q=reusable%20%20cooperative%20catalytic%20system" title=" reusable cooperative catalytic system"> reusable cooperative catalytic system</a>, <a href="https://publications.waset.org/abstracts/search?q=biomimetic%20oxidation%20reaction" title=" biomimetic oxidation reaction"> biomimetic oxidation reaction</a> </p> <a href="https://publications.waset.org/abstracts/150615/co-immobilization-of-palladium-nanoparticles-and-polyoxometalate-into-the-cavities-of-the-mesocellular-foams-a-biomimetic-cooperative-catalytic-system-for-aerobic-oxidation-of-alcohols-under-green-conditions" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/150615.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">118</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">148</span> Cross-Linked Amyloglucosidase Aggregates: A New Carrier Free Immobilization Strategy for Continuous Saccharification of Starch</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sidra%20Pervez">Sidra Pervez</a>, <a href="https://publications.waset.org/abstracts/search?q=Afsheen%20Aman"> Afsheen Aman</a>, <a href="https://publications.waset.org/abstracts/search?q=Shah%20Ali%20Ul%20Qader"> Shah Ali Ul Qader</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The importance of attaining an optimum performance of an enzyme is often a question of devising an effective method for its immobilization. Cross-linked enzyme aggregate (CLEAs) is a new approach for immobilization of enzymes using carrier free strategy. This method is exquisitely simple (involving precipitation of the enzyme from aqueous buffer followed by cross-linking of the resulting physical aggregates of enzyme molecules) and amenable to rapid optimization. Among many industrial enzymes, amyloglucosidase is an important amylolytic enzyme that hydrolyzes alpha (1→4) and alpha (1→6) glycosidic bonds in starch molecule and produce glucose as a sole end product. Glucose liberated by amyloglucosidase can be used for the production of ethanol and glucose syrups. Besides this amyloglucosidase can be widely used in various food and pharmaceuticals industries. For production of amyloglucosidase on commercial scale, filamentous fungi of genera Aspergillus are mostly used because they secrete large amount of enzymes extracellularly. The current investigation was based on isolation and identification of filamentous fungi from genus Aspergillus for the production of amyloglucosidase in submerged fermentation and optimization of cultivation parameters for starch saccharification. Natural isolates were identified as Aspergillus niger KIBGE-IB36, Aspergillus fumigatus KIBGE-IB33, Aspergillus flavus KIBGE-IB34 and Aspergillus terreus KIBGE-IB35 on taxonomical basis and 18S rDNA analysis and their sequence were submitted to GenBank. Among them, Aspergillus fumigatus KIBGE-IB33 was selected on the basis of maximum enzyme production. After optimization of fermentation conditions enzyme was immobilized on CLEA. Different parameters were optimized for maximum immobilization of amyloglucosidase. Data of enzyme stability (thermal and Storage) and reusability suggested the applicability of immobilized amyloglucosidase for continuous saccharification of starch in industrial processes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aspergillus" title="aspergillus">aspergillus</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=industrial%20processes" title=" industrial processes"> industrial processes</a>, <a href="https://publications.waset.org/abstracts/search?q=starch%20saccharification" title=" starch saccharification"> starch saccharification</a> </p> <a href="https://publications.waset.org/abstracts/30962/cross-linked-amyloglucosidase-aggregates-a-new-carrier-free-immobilization-strategy-for-continuous-saccharification-of-starch" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/30962.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">496</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">147</span> Effect of Anion and Amino Functional Group on Resin for Lipase Immobilization with Adsorption-Cross Linking Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Heri%20Hermansyah">Heri Hermansyah</a>, <a href="https://publications.waset.org/abstracts/search?q=Annisa%20Kurnia"> Annisa Kurnia</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Vania%20Anisya"> A. Vania Anisya</a>, <a href="https://publications.waset.org/abstracts/search?q=Adi%20Surjosatyo"> Adi Surjosatyo</a>, <a href="https://publications.waset.org/abstracts/search?q=Yopi%20Sunarya"> Yopi Sunarya</a>, <a href="https://publications.waset.org/abstracts/search?q=Rita%20Arbianti"> Rita Arbianti</a>, <a href="https://publications.waset.org/abstracts/search?q=Tania%20Surya%20Utami"> Tania Surya Utami</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Lipase is one of biocatalyst which is applied commercially for the process in industries, such as bioenergy, food, and pharmaceutical industry. Nowadays, biocatalysts are preferred in industries because they work in mild condition, high specificity, and reduce energy consumption (high pressure and temperature). But, the usage of lipase for industry scale is limited by economic reason due to the high price of lipase and difficulty of the separation system. Immobilization of lipase is one of the solutions to maintain the activity of lipase and reduce separation system in the process. Therefore, we conduct a study about lipase immobilization with the adsorption-cross linking method using glutaraldehyde because this method produces high enzyme loading and stability. Lipase is immobilized on different kind of resin with the various functional group. Highest enzyme loading (76.69%) was achieved by lipase immobilized on anion macroporous which have anion functional group (OH<sup>‑</sup>). However, highest activity (24,69 U/g support) through olive oil emulsion method was achieved by lipase immobilized on anion macroporous-chitosan which have amino (NH<sub>2</sub>) and anion (OH<sup>-</sup>) functional group. In addition, it also success to produce biodiesel until reach yield 50,6% through interesterification reaction and after 4 cycles stable 63.9% relative with initial yield. While for Aspergillus, niger lipase immobilized on anion macroporous-kitosan have unit activity 22,84 U/g resin and yield biodiesel higher than commercial lipase (69,1%) and after 4 cycles stable reach 70.6% relative from initial yield. This shows that optimum functional group on support for immobilization with adsorption-cross linking is the support that contains amino (NH<sub>2</sub>) and anion (OH<sup>-</sup>) functional group because they can react with glutaraldehyde and binding with enzyme prevent desorption of lipase from support through binding lipase with a functional group on support. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=adsorption-cross%20linking" title="adsorption-cross linking">adsorption-cross linking</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=lipase" title=" lipase"> lipase</a>, <a href="https://publications.waset.org/abstracts/search?q=resin" title=" resin"> resin</a> </p> <a href="https://publications.waset.org/abstracts/33854/effect-of-anion-and-amino-functional-group-on-resin-for-lipase-immobilization-with-adsorption-cross-linking-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/33854.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">369</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">146</span> Improvement of Activity of β-galactosidase from Kluyveromyces lactis via Immobilization on Polyethylenimine-Chitosan</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Carlos%20A.%20C.%20G.%20Neto">Carlos A. C. G. Neto</a>, <a href="https://publications.waset.org/abstracts/search?q=Natan%20C.%20G.%20e%20Silva"> Natan C. G. e Silva </a>, <a href="https://publications.waset.org/abstracts/search?q=Tha%C3%ADs%20de%20O.%20Costa"> Thaís de O. Costa</a>, <a href="https://publications.waset.org/abstracts/search?q=Luciana%20R.%20B.%20Gon%C3%A7alves"> Luciana R. B. Gonçalves</a>, <a href="https://publications.waset.org/abstracts/search?q=Maria%20V.%20P.%20Rocha"> Maria V. P. Rocha</a> </p> <p class="card-text"><strong>Abstract:</strong></p> β-galactosidases (E.C. 3.2.1.23) are enzymes that have attracted by catalyzing the hydrolysis of lactose and in producing galacto-oligosaccharides by favoring transgalactosylation reactions. These enzymes, when immobilized, can have some enzymatic characteristics substantially improved, and the coating of supports with multifunctional polymers is a promising alternative to enhance the stability of the biocatalysts, among which polyethylenimine (PEI) stands out. PEI has certain properties, such as being a flexible polymer that suits the structure of the enzyme, giving greater stability, especially for multimeric enzymes such as β-galactosidases. Besides that, protects them from environmental variations. The use of chitosan support coated with PEI could improve the catalytic efficiency of β-galactosidase from Kluyveromyces lactis in the transgalactosylation reaction for the production of prebiotics, such as lactulose since this strain is more effective in the hydrolysis reaction. In this context, the aim of the present work was first to develop biocatalysts of β-galactosidase from K. lactis immobilized on chitosan-coated with PEI, determining the immobilization parameters, its operational and thermal stability, and then to apply it in hydrolysis and transgalactolisation reactions to produce lactulose using whey as a substrate. The immobilization of β-galactosidase in chitosan previously functionalized with 0.8% (v/v) glutaraldehyde and then coated with 10% (w/v) PEI solution was evaluated using an enzymatic load of 10 mg protein per gram support. Subsequently, the hydrolysis and transgalactosylation reactions were conducted at 50 °C, 120 RPM for 20 minutes, using whey supplemented with fructose at a ratio of 1:2 lactose/fructose, totaling 200 g/L. Operational stability studies were performed in the same conditions for 10 cycles. Thermal stabilities of biocatalysts were conducted at 50 ºC in 50 mM phosphate buffer, pH 6.6 with 0.1 mM MnCl2. The biocatalyst whose support was coated was named CHI_GLU_PEI_GAL, and the one that was not coated was named CHI_GLU_GAL. The coating of the support with PEI considerably improved the parameters of immobilization. The immobilization yield increased from 56.53% to 97.45%, biocatalyst activity from 38.93 U/g to 95.26 U/g and the efficiency from 3.51% to 6.0% for uncoated and coated support, respectively. The biocatalyst CHI_GLU_PEI_GAL was better than CHI_GLU_GAL in the hydrolysis of lactose and production of lactulose, converting 97.05% of lactose at 5 min of reaction and producing 7.60 g/L lactulose in the same time interval. QUI_GLU_PEI_GAL biocatalyst was stable in the hydrolysis reactions of lactose during the 10 cycles evaluated, converting 73.45% lactose even after the tenth cycle, and in the lactulose production was stable until the fifth cycle evaluated, producing 10.95 g/L lactulose. However, the thermal stability of CHI_GLU_GAL biocatalyst was superior, with a half-life time 6 times higher, probably because the enzyme was immobilized by covalent bonding, which is stronger than adsorption (CHI_GLU_PEI_GAL). Therefore, the strategy of coating the supports with PEI has proven to be effective for the immobilization of β-galactosidase from K. lactis, considerably improving the immobilization parameters, as well as, the catalytic action of the enzyme. Besides that, this process can be economically viable due to the use of an industrial residue as a substrate. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=%CE%B2-galactosidase" title="β-galactosidase">β-galactosidase</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=kluyveromyces%20lactis" title=" kluyveromyces lactis"> kluyveromyces lactis</a>, <a href="https://publications.waset.org/abstracts/search?q=lactulose" title=" lactulose"> lactulose</a>, <a href="https://publications.waset.org/abstracts/search?q=polyethylenimine" title=" polyethylenimine"> polyethylenimine</a>, <a href="https://publications.waset.org/abstracts/search?q=transgalactosylation%20reaction" title=" transgalactosylation reaction"> transgalactosylation reaction</a>, <a href="https://publications.waset.org/abstracts/search?q=whey" title=" whey"> whey</a> </p> <a href="https://publications.waset.org/abstracts/120647/improvement-of-activity-of-v-galactosidase-from-kluyveromyces-lactis-via-immobilization-on-polyethylenimine-chitosan" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/120647.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">145</span> Successful Immobilization of Alcohol Dehydrogenase on Natural and Synthetic Support and Its Reaction on Ethanol</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hiral%20D.%20Trivedi">Hiral D. Trivedi</a>, <a href="https://publications.waset.org/abstracts/search?q=Dinesh%20S.%20Patel"> Dinesh S. Patel</a>, <a href="https://publications.waset.org/abstracts/search?q=Sachin%20P.%20Shukla"> Sachin P. Shukla</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We have immobilized alcohol dehydrogenase on k-carrageenan, which is a natural polysaccharide obtained from seaweeds by entrapment and on copolymer of acrylamide and 2-hydroxy ethylmethaacrylate by covalent coupling. We have optimized all the immobilization parameters and also carried the comparison studies of both. In case of copolymer of acrylamide and 2-hydroxy ethylmethaacrylate, we have activated both the amino and hydroxyl group individually and simultaneously using different activating agents and obtained some interesting results. We have found that covalently bound enzyme was found to be better under all tested conditions. The reaction on ethanol was carried out using these immobilized systems. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alcohol%20dehydrogenase" title="alcohol dehydrogenase">alcohol dehydrogenase</a>, <a href="https://publications.waset.org/abstracts/search?q=acrylamide-co-2-hydroxy%20ethylmethaacrylate" title=" acrylamide-co-2-hydroxy ethylmethaacrylate"> acrylamide-co-2-hydroxy ethylmethaacrylate</a>, <a href="https://publications.waset.org/abstracts/search?q=ethanol" title=" ethanol"> ethanol</a>, <a href="https://publications.waset.org/abstracts/search?q=k-carrageenan" title=" k-carrageenan"> k-carrageenan</a> </p> <a href="https://publications.waset.org/abstracts/118413/successful-immobilization-of-alcohol-dehydrogenase-on-natural-and-synthetic-support-and-its-reaction-on-ethanol" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/118413.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">146</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">144</span> Reusability of Coimmobilized Enzymes</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Aleksandra%20%C5%81ochowicz">Aleksandra Łochowicz</a>, <a href="https://publications.waset.org/abstracts/search?q=Daria%20%C5%9Awi%C4%99tochowska"> Daria Świętochowska</a>, <a href="https://publications.waset.org/abstracts/search?q=Loredano%20Pollegioni"> Loredano Pollegioni</a>, <a href="https://publications.waset.org/abstracts/search?q=Nazim%20Ocal"> Nazim Ocal</a>, <a href="https://publications.waset.org/abstracts/search?q=Franck%20Charmantray"> Franck Charmantray</a>, <a href="https://publications.waset.org/abstracts/search?q=Laurence%20Hecquet"> Laurence Hecquet</a>, <a href="https://publications.waset.org/abstracts/search?q=Katarzyna%20Szyma%C5%84ska"> Katarzyna Szymańska</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Multienzymatic cascade reactions are nowadays widely used in pharmaceutical, chemical and cosmetics industries to produce high valuable compounds. They can be carried out in two ways, step by step and one-pot. If two or more enzymes are in the same reaction vessel is necessary to work out the compromise to run the reaction in optimal conditions for each enzyme. So far most of the reports of multienzymatic cascades concern on usage of free enzymes. Unfortunately using free enzymes as catalysts of reactions accomplish high cost. What is more, free enzymes are soluble in solvents which makes reuse impossible. To overcome this obstacle enzymes can be immobilized what provides heterogeneity of biocatalyst that enables reuse and easy separation of the enzyme from solvents and reaction products. Usually, immobilization increase also the thermal and operational stability of enzyme. The advantages of using immobilized multienzymes are enhanced enzyme stability, improved cascade enzymatic activity via substrate channeling, and ease of recovery for reuse. The one-pot immobilized multienzymatic cascade can be carried out in mixed or coimmobilized type. When biocatalysts are coimmobilized on the same carrier the are in close contact to each other which increase the reaction rate and catalytic efficiency, and eliminate the lag time. However, in this type providing the optimal conditions both in the process of immobilization and cascade reaction for each enzyme is complicated. Herein, we examined immobilization of 3 enzymes: D-amino acid oxidase from Rhodotorula gracilis, commercially available catalase and transketolase from Geobacillus stearothermophilus. As a support we used silica monoliths with hierarchical structure of pores. Then we checked their stability and reusability in one-pot cascade of L-erythrulose and hydroxypuryvate acid synthesis. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biocatalysts" title="biocatalysts">biocatalysts</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20immobilization" title=" enzyme immobilization"> enzyme immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=multienzymatic%20reaction" title=" multienzymatic reaction"> multienzymatic reaction</a>, <a href="https://publications.waset.org/abstracts/search?q=silica%20carriers" title=" silica carriers"> silica carriers</a> </p> <a href="https://publications.waset.org/abstracts/152282/reusability-of-coimmobilized-enzymes" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/152282.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">150</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">143</span> Enzyme Immobilization on Functionalized Polystyrene Nanofibersfor Bioprocessing Applications</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mailin%20Misson">Mailin Misson</a>, <a href="https://publications.waset.org/abstracts/search?q=Bo%20Jin"> Bo Jin</a>, <a href="https://publications.waset.org/abstracts/search?q=Sheng%20Dai"> Sheng Dai</a>, <a href="https://publications.waset.org/abstracts/search?q=Hu%20Zhang"> Hu Zhang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Advances in biotechnology have witnessed a growing interest in enzyme applications for the development of green and sustainable bio processes. While known as powerful bio catalysts, enzymes are no longer of economic value when extended to large commercialization. Alternatively, immobilization technology allows enzyme recovery and continuous reuse which subsequently compensates high operating costs. Employment of enzymes on nano structured materials has been recognized as a promising approach to enhance enzyme catalytic performances. High porosity, inter connectivity and self-assembling behaviors endow nano fibers as exciting candidate for enzyme carrier in bio reactor systems. In this study, nano fibers were successfully fabricated via electro spinning system by optimizing the polymer concentration (10-30 %, w/v), applied voltage (10-30 kV) and discharge distance (11-26 cm). Microscopic images have confirmed the quality as homogeneous and good fiber alignment. The nano fibers surface was modified using strong oxidizing agent to facilitate bio molecule binding. Bovine serum albumin and β-galactosidase enzyme were employed as model bio catalysts and immobilized onto the oxidized surfaces through covalent binding. Maximum enzyme adsorption capacity of the modified nano fibers was 3000 mg/g, 3-fold higher than the unmodified counterpart (1000 mg/g). The highest immobilization yield was 80% and reached the saturation point at 2 mg/ml of enzyme concentration. The results indicate a significant increase of activity retention by the enzyme-bound modified nano fibers (80%) as compared to the nascent one (60%), signifying excellent enzyme-nano carrier bio compatibility. The immobilized enzyme was further used for the bio conversion of dairy wastes into value-added products. This study demonstrates great potential of acid-modified electrospun polystyrene nano fibers as enzyme carriers. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=immobilization" title="immobilization">immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme" title=" enzyme"> enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=nanocarrier" title=" nanocarrier"> nanocarrier</a>, <a href="https://publications.waset.org/abstracts/search?q=nanofibers" title=" nanofibers"> nanofibers</a> </p> <a href="https://publications.waset.org/abstracts/15802/enzyme-immobilization-on-functionalized-polystyrene-nanofibersfor-bioprocessing-applications" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/15802.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">293</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">142</span> Rule of Natural Synthetic Chemical on Lead Immobilization in Polluted Sandy Soils </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Saud%20S.%20AL%20Oud">Saud S. AL Oud</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Soil contamination can have dire consequences, such as loss of ecosystem and agricultural productivity, diminished food chain quality, tainted water resources, economic loss, and human and animal illness. In recent years, attention has focused on the development of in situ immobilization methods that are generally less expensive and disruptive to the natural landscape, hydrology, and ecosystems than are conventional excavation treatments, and disposal methods. Soft, inexpensive, and efficient agents were used in the present research to immobilize Pb in polluted sandy soil. Five agents, either naturally occurring or chemically prepared, were used for this purpose. These agents include; iron ore (72% Fe2O3), cement, a mixture of calcite and shale rich in aluminum (CASH), and two chemically prepared amorphous materials of Al- and Fe-gel. These agents were selected due to their ability to specifically adsorb heavy metals onto their surface OH functional groups, which provide permanent immobilization of metal pollutants and reduce the fraction that is potentially mobile or bioavailable. The efficiency of these agents in immobilizing Pb were examined in a laboratory experiment, in which two rates (0.5 and 1.0 %) of tested agents were added to the polluted soils containing total contents of Pb ranging from 17.4-49.8 mg/kg. The results show that all immobilizing agents were succeed in minimizing the mobile form of Pb as extracted by 0.5 N HNO3. The extracted Pb decreased with increasing addition rate of immobilizing agents. At addition rate of 0.5%, HNO3 extractable-Pb varied widely depending on the agents type and were found to represent 21-67% of the initial values. All agents were able to reduce mobile Pb to levels lower than that (2.0 mg/kg) reported for non polluted soil, particularly for soils had initials of mobile Pb less than 10 mg/kg. Both iron oxide and CASH had the highest efficiency in immobilizing Pb, followed by cement, then amorphous materials of Fe and Al hydroxides. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=soil" title="soil">soil</a>, <a href="https://publications.waset.org/abstracts/search?q=synthetic%20chemical" title=" synthetic chemical"> synthetic chemical</a>, <a href="https://publications.waset.org/abstracts/search?q=lead" title=" lead"> lead</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=polluted" title=" polluted "> polluted </a> </p> <a href="https://publications.waset.org/abstracts/18023/rule-of-natural-synthetic-chemical-on-lead-immobilization-in-polluted-sandy-soils" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/18023.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">141</span> Inulinase Immobilization on Functionalized Magnetic Nanoparticles Prepared with Soy Protein Isolate Conjugated Bovine Serum Albumin for High Fructose Syrup Production</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Homa%20Torabizadeh">Homa Torabizadeh</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohaddeseh%20Mikani"> Mohaddeseh Mikani </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Inulinase from <em>Aspergillus niger</em> was covalently immobilized on magnetic nanoparticles (MNPs/Fe<sub>3</sub>O<sub>4</sub>) covered with soy protein isolate (SPI/Fe<sub>3</sub>O<sub>4</sub>) functionalized by bovine serum albumin (BSA) nanoparticles. MNPs are promising enzyme carriers because they separate easily under external magnetic fields and have enhanced immobilized enzyme reusability. As MNPs aggregate simply, surface coating strategy was employed. SPI functionalized by BSA was a suitable candidate for nanomagnetite coating due to its superior biocompatibility and hydrophilicity. Fe<sub>3</sub>O<sub>4</sub>@SPI-BSA nanoparticles were synthesized as a novel carrier with narrow particle size distribution. Step by step fabrication monitoring of Fe<sub>3</sub>O<sub>4</sub>@SPI-BSA nanoparticles was performed using field emission scanning electron microscopy and dynamic light scattering. The results illustrated that nanomagnetite with the spherical morphology was well monodispersed with the diameter of about 35 nm. The average size of the SPI-BSA nanoparticles was 80 to 90 nm, and their zeta potential was around −34 mV. Finally, the mean diameter of fabricated Fe<sub>3</sub>O<sub>4</sub>@SPI-BSA NPs was less than 120 nm. Inulinase enzyme from <em>Aspergillus niger</em> was covalently immobilized through gluteraldehyde on Fe<sub>3</sub>O<sub>4</sub>@SPI-BSA nanoparticles successfully. Fourier transform infrared spectra and field emission scanning electron microscopy images provided sufficient proof for the enzyme immobilization on the nanoparticles with 80% enzyme loading. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=high%20fructose%20syrup" title="high fructose syrup">high fructose syrup</a>, <a href="https://publications.waset.org/abstracts/search?q=inulinase%20immobilization" title=" inulinase immobilization"> inulinase immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=functionalized%20magnetic%20nanoparticles" title=" functionalized magnetic nanoparticles"> functionalized magnetic nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=soy%20protein%20isolate" title=" soy protein isolate"> soy protein isolate</a> </p> <a href="https://publications.waset.org/abstracts/68691/inulinase-immobilization-on-functionalized-magnetic-nanoparticles-prepared-with-soy-protein-isolate-conjugated-bovine-serum-albumin-for-high-fructose-syrup-production" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/68691.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">299</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">140</span> Introduction of PMMA-Tag to VHH for Improving Recovery and Immobilization Rate of VHHS</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bongmun%20Kang">Bongmun Kang</a>, <a href="https://publications.waset.org/abstracts/search?q=Kagnari%20Yamakawa"> Kagnari Yamakawa</a>, <a href="https://publications.waset.org/abstracts/search?q=Yoshihisa%20Hagihara"> Yoshihisa Hagihara</a>, <a href="https://publications.waset.org/abstracts/search?q=Yuji%20Ito"> Yuji Ito</a>, <a href="https://publications.waset.org/abstracts/search?q=Michimasa%20Kishimoto"> Michimasa Kishimoto</a>, <a href="https://publications.waset.org/abstracts/search?q=Yoichi%20Kumada"> Yoichi Kumada</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The PMMA-tag was genetically fused with the C-terminal region of VHH molecules. This antibody, VHH, is known as a single-chain domain, which is devoid of light chains. The PMMA-tag, which could affect the isoelectric point (pI) changeable with a charge of amino acid in VHHs were closely related to the solubility of VHH molecules during refolding. The genetic fusion of PMMA-tag to C-terminal region of VHHs significantly affects the recovery of their soluble protein during refolding by 50 mM TAPS at pH 8.5. It could be refolded with a recovery of more than 95% by dialysis at pH 8.5. A marked difference in the antigen-binding activities in the adsorption state was significantly high in VHH-PM compared to the wild type of VHH. There are approximately 8-fold differences in the antigen-binding activities in the adsorption state between VHH-PM and VHH. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=VHH" title="VHH">VHH</a>, <a href="https://publications.waset.org/abstracts/search?q=PMMA-tag" title=" PMMA-tag"> PMMA-tag</a>, <a href="https://publications.waset.org/abstracts/search?q=isoelectric%20point" title=" isoelectric point"> isoelectric point</a>, <a href="https://publications.waset.org/abstracts/search?q=pH" title=" pH"> pH</a>, <a href="https://publications.waset.org/abstracts/search?q=Solubility" title=" Solubility"> Solubility</a>, <a href="https://publications.waset.org/abstracts/search?q=refolding" title=" refolding"> refolding</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=ELISA" title=" ELISA"> ELISA</a> </p> <a href="https://publications.waset.org/abstracts/19089/introduction-of-pmma-tag-to-vhh-for-improving-recovery-and-immobilization-rate-of-vhhs" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/19089.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">419</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">139</span> Improved Reuse and Storage Performances at Room Temperature of a New Environmental-Friendly Lactate Oxidase Biosensor Made by Ambient Electrospray Deposition</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Antonella%20Cartoni">Antonella Cartoni</a>, <a href="https://publications.waset.org/abstracts/search?q=Mattea%20Carmen%20Castrovilli"> Mattea Carmen Castrovilli</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A biosensor for lactate detection has been developed using an environmentally friendly approach. The biosensor is based on lactate oxidase (LOX) and has remarkable capabilities for reuse and storage at room temperature. The manufacturing technique employed is ambient electrospray deposition (ESD), which enables efficient and sustainable immobilization of the LOX enzyme on a cost-effective com-mercial screen-printed Prussian blue/carbon electrode (PB/C-SPE). The study demonstrates that the ESD technology allows the biosensor to be stored at ambient pressure and temperature for extended periods without affecting the enzymatic activity. The biosensor can be stored for up to 90 days without requiring specific storage conditions, and it can be reused for up to 24 measurements on both freshly prepared electrodes and electrodes that are three months old. The LOX-based biosensor exhibits a lin-ear range of lactate detection between 0.1 and 1 mM, with a limit of detection of 0.07±0.02 mM. Ad-ditionally, it does not exhibit any memory effects. The immobilization process does not involve the use of entrapment matrices or hazardous chemicals, making it environmentally sustainable and non-toxic compared to current methods. Furthermore, the application of a electrospray deposition cycle on previously used biosensors rejuvenates their performance, making them comparable to freshly made biosensors. This highlights the excellent recycling potential of the technique, eliminating the waste as-sociated with disposable devices. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=green%20friendly" title="green friendly">green friendly</a>, <a href="https://publications.waset.org/abstracts/search?q=reuse" title=" reuse"> reuse</a>, <a href="https://publications.waset.org/abstracts/search?q=storage%20performance" title=" storage performance"> storage performance</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=matrix-free" title=" matrix-free"> matrix-free</a>, <a href="https://publications.waset.org/abstracts/search?q=electrospray%20deposition" title=" electrospray deposition"> electrospray deposition</a>, <a href="https://publications.waset.org/abstracts/search?q=biosensor" title=" biosensor"> biosensor</a>, <a href="https://publications.waset.org/abstracts/search?q=lactate%20oxidase" title=" lactate oxidase"> lactate oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme" title=" enzyme"> enzyme</a> </p> <a href="https://publications.waset.org/abstracts/175645/improved-reuse-and-storage-performances-at-room-temperature-of-a-new-environmental-friendly-lactate-oxidase-biosensor-made-by-ambient-electrospray-deposition" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/175645.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">65</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">138</span> Cell-free Bioconversion of n-Octane to n-Octanol via a Heterogeneous and Bio-Catalytic Approach</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shanna%20Swart">Shanna Swart</a>, <a href="https://publications.waset.org/abstracts/search?q=Caryn%20Fenner"> Caryn Fenner</a>, <a href="https://publications.waset.org/abstracts/search?q=Athanasios%20Kotsiopoulos"> Athanasios Kotsiopoulos</a>, <a href="https://publications.waset.org/abstracts/search?q=Susan%20Harrison"> Susan Harrison</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Linear alkanes are produced as by-products from the increasing use of gas-to-liquid fuel technologies for synthetic fuel production and offer great potential for value addition. Their current use as low-value fuels and solvents do not maximize this potential. Therefore, attention has been drawn towards direct activation of these aliphatic alkanes to more useful products such as alcohols, aldehydes, carboxylic acids and derivatives. Cytochrome P450 monooxygenases (P450s) can be used for activation of these aliphatic alkanes using whole-cells or cell-free systems. Some limitations of whole-cell systems include reduced mass transfer, stability and possible side reactions. Since the P450 systems are little studied as cell-free systems, they form the focus of this study. Challenges of a cell-free system include co-factor regeneration, substrate availability and enzyme stability. Enzyme immobilization offers a positive outlook on this dilemma, as it may enhance stability of the enzyme. In the present study, 2 different P450s (CYP153A6 and CYP102A1) as well as the relevant accessory enzymes required for electron transfer (ferredoxin and ferredoxin reductase) and co-factor regeneration (glucose dehydrogenase) have been expressed in E. coli and purified by metal affinity chromatography. Glucose dehydrogenase (GDH), was used as a model enzyme to assess the potential of various enzyme immobilization strategies including; surface attachment on MagReSyn® microspheres with various functionalities and on electrospun nanofibers, using self-assembly based methods forming Cross Linked Enzymes (CLE), Cross Linked Enzyme Aggregates (CLEAs) and spherezymes as well as in a sol gel. The nanofibers were synthesized by electrospinning, which required the building of an electrospinning machine. The nanofiber morphology has been analyzed by SEM and binding will be further verified by FT-IR. Covalent attachment based methods showed limitations where only ferredoxin reductase and GDH retained activity after immobilization which were largely attributed to insufficient electron transfer and inactivation caused by the crosslinkers (60% and 90% relative activity loss for the free enzyme when using 0.5% glutaraldehyde and glutaraldehyde/ethylenediamine (1:1 v/v), respectively). So far, initial experiments with GDH have shown the most potential when immobilized via their His-tag onto the surface of MagReSyn® microspheres functionalized with Ni-NTA. It was found that Crude GDH could be simultaneously purified and immobilized with sufficient activity retention. Immobilized pure and crude GDH could be recycled 9 and 10 times, respectively, with approximately 10% activity remaining. The immobilized GDH was also more stable than the free enzyme after storage for 14 days at 4˚C. This immobilization strategy will also be applied to the P450s and optimized with regards to enzyme loading and immobilization time, as well as characterized and compared with the free enzymes. It is anticipated that the proposed immobilization set-up will offer enhanced enzyme stability (as well as reusability and easy recovery), minimal mass transfer limitation, with continuous co-factor regeneration and minimal enzyme leaching. All of which provide a positive outlook on this robust multi-enzyme system for efficient activation of linear alkanes as well as the potential for immobilization of various multiple enzymes, including multimeric enzymes for different bio-catalytic applications beyond alkane activation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alkane%20activation" title="alkane activation">alkane activation</a>, <a href="https://publications.waset.org/abstracts/search?q=cytochrome%20P450%20monooxygenase" title=" cytochrome P450 monooxygenase"> cytochrome P450 monooxygenase</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20catalysis" title=" enzyme catalysis"> enzyme catalysis</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20immobilization" title=" enzyme immobilization"> enzyme immobilization</a> </p> <a href="https://publications.waset.org/abstracts/71470/cell-free-bioconversion-of-n-octane-to-n-octanol-via-a-heterogeneous-and-bio-catalytic-approach" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/71470.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">227</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">137</span> The Effect of Immobilization Conditions on Hydrogen Production from Palm Oil Mill Effluent</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20W.%20Zularisam">A. W. Zularisam</a>, <a href="https://publications.waset.org/abstracts/search?q=Lakhveer%20Singh"> Lakhveer Singh</a>, <a href="https://publications.waset.org/abstracts/search?q=Mimi%20Sakinah%20Abdul%20Munaim"> Mimi Sakinah Abdul Munaim </a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this study, the optimization of hydrogen production using polyethylene glycol (PEG) immobilized sludge was investigated in batch tests. Palm oil mill effluent (POME) is used as a substrate that can act as a carbon source. Experiment focus on the effect of some important affecting factors on fermentative hydrogen production. Results showed that immobilized sludge demonstrated the maximum hydrogen production rate of 340 mL/L-POME/h under follow optimal condition: amount of biomass 10 mg VSS/ g bead, PEG concentration 10%, and cell age 24 h or 40 h. More importantly, immobilized sludge not only enhanced hydrogen production but can also tolerate the harsh environment and produce hydrogen at the wide ranges of pH. The present results indicate the potential of PEG-immobilized sludge for large-scale operations as well; these factors play an important role in stable and continuous hydrogen production. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=bioydrogen" title="bioydrogen">bioydrogen</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=polyethylene%20glycol" title=" polyethylene glycol"> polyethylene glycol</a>, <a href="https://publications.waset.org/abstracts/search?q=palm%20oil%20mill%20effluent" title=" palm oil mill effluent"> palm oil mill effluent</a>, <a href="https://publications.waset.org/abstracts/search?q=dark%20fermentation" title=" dark fermentation "> dark fermentation </a> </p> <a href="https://publications.waset.org/abstracts/39206/the-effect-of-immobilization-conditions-on-hydrogen-production-from-palm-oil-mill-effluent" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/39206.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">343</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">136</span> Functionalization of Carbon-Coated Iron Nanoparticles with Fluorescent Protein</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20G.%20Pershina">A. G. Pershina</a>, <a href="https://publications.waset.org/abstracts/search?q=P.%20S.%20Postnikov"> P. S. Postnikov</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20E.%20Trusova"> M. E. Trusova</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20O.%20Burlakova"> D. O. Burlakova</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20E.%20Sazonov"> A. E. Sazonov</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Invention of magnetic-fluorescent nanocomposites is a rapidly developing area of research. The magnetic-fluorescent nanocomposite attractiveness is connected with the ability of simultaneous management and control of such nanocomposites by two independent methods based on different physical principles. These nanocomposites are applied for the solution of various essential scientific and experimental biomedical problems. The aim of this research is development of principle approach to nanobiohybrid structures with magnetic and fluorescent properties design. The surface of carbon-coated iron nanoparticles (Fe@C) were covalently modified by 4-carboxy benzenediazonium tosylate. Recombinant fluorescent protein TagGFP2 (Eurogen) was obtained in E. coli (Rosetta DE3) by standard laboratory techniques. Immobilization of TagGFP2 on the nanoparticles surface was provided by the carbodiimide activation. The amount of COOH-groups on the nanoparticle surface was estimated by elemental analysis (Elementar Vario Macro) and TGA-analysis (SDT Q600, TA Instruments. Obtained nanocomposites were analyzed by FTIR spectroscopy (Nicolet Thermo 5700) and fluorescence microscopy (AxioImager M1, Carl Zeiss). Amount of the protein immobilized on the modified nanoparticle surface was determined by fluorimetry (Cary Eclipse) and spectrophotometry (Unico 2800) with the help of preliminary obtained calibration plots. In the FTIR spectra of modified nanoparticles the adsorption band of –COOH group around 1700 cm-1 and bands in the region of 450-850 cm-1 caused by bending vibrations of benzene ring were observed. The calculated quantity of active groups on the surface was equal to 0,1 mmol/g of material. The carbodiimide activation of COOH-groups on nanoparticles surface results to covalent immobilization of TagGFP2 fluorescent protein (0.2 nmol/mg). The success of immobilization was proved by FTIR spectroscopy. Protein characteristic adsorption bands in the region of 1500-1600 cm-1 (amide I) were presented in the FTIR spectrum of nanocomposite. The fluorescence microscopy analysis shows that Fe@C-TagGFP2 nanocomposite possesses fluorescence properties. This fact confirms that TagGFP2 protein retains its conformation due to immobilization on nanoparticles surface. Magnetic-fluorescent nanocomposite was obtained as a result of unique design solution implementation – the fluorescent protein molecules were fixed to the surface of superparamagnetic carbon-coated iron nanoparticles using original diazonium salts. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=carbon-coated%20iron%20nanoparticles" title="carbon-coated iron nanoparticles">carbon-coated iron nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=diazonium%20salts" title=" diazonium salts"> diazonium salts</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent%20protein" title=" fluorescent protein"> fluorescent protein</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a> </p> <a href="https://publications.waset.org/abstracts/7691/functionalization-of-carbon-coated-iron-nanoparticles-with-fluorescent-protein" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/7691.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">342</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">135</span> Brewing in a Domestic Refrigerator Using Freeze-Dried Raw Materials </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Angelika-Ioanna%20Gialleli">Angelika-Ioanna Gialleli</a>, <a href="https://publications.waset.org/abstracts/search?q=Gousi%20Mantha"> Gousi Mantha</a>, <a href="https://publications.waset.org/abstracts/search?q=Maria%20Kanellaki"> Maria Kanellaki</a>, <a href="https://publications.waset.org/abstracts/search?q=Bekatorou%20Argyro"> Bekatorou Argyro</a>, <a href="https://publications.waset.org/abstracts/search?q=Athanasios%20Koutinas"> Athanasios Koutinas</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this study, a new brewing technology with dry raw materials is proposed with potential application in home brewing. Bio catalysts were prepared by immobilization of the psychrotolerant yeast strain Saccharomyces cerevisiae AXAZ-1 on tubular cellulose. Both the word and the biocatalysts were freeze-dried without any cryoprotectants and used for low temperature brewing. The combination of immobilization and freeze-drying techniques was applied successfully, giving a potential for supplying breweries with preserved and ready-to-use immobilized cells. The effect of wort sugar concentration (7°, 8.5°, 10°Be), temperature (2, 5, 7° C) and carrier concentration (5, 10, 20 g/L) on fermentation kinetics and final product quality (volatiles, colour, polyphenols, bitterness) was assessed. The same procedure was repeated with free cells for comparison of the results. The results for immobilized cells were better compared to free cells regarding fermentation kinetics and organoleptic characteristics. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=brewing" title="brewing">brewing</a>, <a href="https://publications.waset.org/abstracts/search?q=tubular%20cellulose" title=" tubular cellulose"> tubular cellulose</a>, <a href="https://publications.waset.org/abstracts/search?q=low%20temperature" title=" low temperature"> low temperature</a>, <a href="https://publications.waset.org/abstracts/search?q=biocatalyst" title=" biocatalyst"> biocatalyst</a> </p> <a href="https://publications.waset.org/abstracts/15780/brewing-in-a-domestic-refrigerator-using-freeze-dried-raw-materials" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/15780.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">323</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">134</span> ENDO-β-1,4-Xylanase from Thermophilic Geobacillus stearothermophilus: Immobilization Using Matrix Entrapment Technique to Increase the Stability and Recycling Efficiency</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Afsheen%20Aman">Afsheen Aman</a>, <a href="https://publications.waset.org/abstracts/search?q=Zainab%20Bibi"> Zainab Bibi</a>, <a href="https://publications.waset.org/abstracts/search?q=Shah%20Ali%20Ul%20Qader"> Shah Ali Ul Qader</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Introduction: Xylan is a heteropolysaccharide composed of xylose monomers linked together through 1,4 linkages within a complex xylan network. Owing to wide applications of xylan hydrolytic products (xylose, xylobiose and xylooligosaccharide) the researchers are focusing towards the development of various strategies for efficient xylan degradation. One of the most important strategies focused is the use of heat tolerant biocatalysts which acts as strong and specific cleaving agents. Therefore, the exploration of microbial pool from extremely diversified ecosystem is considerably vital. Microbial populations from extreme habitats are keenly explored for the isolation of thermophilic entities. These thermozymes usually demonstrate fast hydrolytic rate, can produce high yields of product and are less prone to microbial contamination. Another possibility of degrading xylan continuously is the use of immobilization technique. The current work is an effort to merge both the positive aspects of thermozyme and immobilization technique. Methodology: Geobacillus stearothermophilus was isolated from soil sample collected near the blast furnace site. This thermophile is capable of producing thermostable endo-β-1,4-xylanase which cleaves xylan effectively. In the current study, this thermozyme was immobilized within a synthetic and a non-synthetic matrice for continuous production of metabolites using entrapment technique. The kinetic parameters of the free and immobilized enzyme were studied. For this purpose calcium alginate and polyacrylamide beads were prepared. Results: For the synthesis of immobilized beads, sodium alginate (40.0 gL-1) and calcium chloride (0.4 M) was used amalgamated. The temperature (50°C) and pH (7.0) optima of immobilized enzyme remained same for xylan hydrolysis however, the enzyme-substrate catalytic reaction time raised from 5.0 to 30.0 minutes as compared to free counterpart. Diffusion limit of high molecular weight xylan (corncob) caused a decline in Vmax of immobilized enzyme from 4773 to 203.7 U min-1 whereas, Km value increased from 0.5074 to 0.5722 mg ml-1 with reference to free enzyme. Immobilized endo-β-1,4-xylanase showed its stability at high temperatures as compared to free enzyme. It retained 18% and 9% residual activity at 70°C and 80°C, respectively whereas; free enzyme completely lost its activity at both temperatures. The Immobilized thermozyme displayed sufficient recycling efficiency and can be reused up to five reaction cycles, indicating that this enzyme can be a plausible candidate in paper processing industry. Conclusion: This thermozyme showed better immobilization yield and operational stability with the purpose of hydrolyzing the high molecular weight xylan. However, the enzyme immobilization properties can be improved further by immobilizing it on different supports for industrial purpose. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=immobilization" title="immobilization">immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=reusability" title=" reusability"> reusability</a>, <a href="https://publications.waset.org/abstracts/search?q=thermozymes" title=" thermozymes"> thermozymes</a>, <a href="https://publications.waset.org/abstracts/search?q=xylanase" title=" xylanase"> xylanase</a> </p> <a href="https://publications.waset.org/abstracts/31636/endo-v-14-xylanase-from-thermophilic-geobacillus-stearothermophilus-immobilization-using-matrix-entrapment-technique-to-increase-the-stability-and-recycling-efficiency" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/31636.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">374</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=immobilization%20of%20fructosyltransferase&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=immobilization%20of%20fructosyltransferase&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=immobilization%20of%20fructosyltransferase&page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=immobilization%20of%20fructosyltransferase&page=5">5</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=immobilization%20of%20fructosyltransferase&page=6">6</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=immobilization%20of%20fructosyltransferase&page=2" rel="next">&rsaquo;</a></li> </ul> </div> </main> <footer> <div id="infolinks" class="pt-3 pb-2"> <div class="container"> <div style="background-color:#f5f5f5;" class="p-3"> <div class="row"> <div class="col-md-2"> <ul class="list-unstyled"> About <li><a href="https://waset.org/page/support">About Us</a></li> <li><a href="https://waset.org/page/support#legal-information">Legal</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/WASET-16th-foundational-anniversary.pdf">WASET celebrates its 16th foundational anniversary</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Account <li><a href="https://waset.org/profile">My Account</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Explore <li><a href="https://waset.org/disciplines">Disciplines</a></li> <li><a href="https://waset.org/conferences">Conferences</a></li> <li><a href="https://waset.org/conference-programs">Conference Program</a></li> <li><a href="https://waset.org/committees">Committees</a></li> <li><a href="https://publications.waset.org">Publications</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Research <li><a href="https://publications.waset.org/abstracts">Abstracts</a></li> <li><a href="https://publications.waset.org">Periodicals</a></li> <li><a href="https://publications.waset.org/archive">Archive</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Open Science <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Philosophy.pdf">Open Science Philosophy</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Award.pdf">Open Science Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Society-Open-Science-and-Open-Innovation.pdf">Open Innovation</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Postdoctoral-Fellowship-Award.pdf">Postdoctoral Fellowship Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Scholarly-Research-Review.pdf">Scholarly Research Review</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Support <li><a href="https://waset.org/page/support">Support</a></li> <li><a href="https://waset.org/profile/messages/create">Contact Us</a></li> <li><a href="https://waset.org/profile/messages/create">Report Abuse</a></li> </ul> </div> </div> </div> </div> </div> <div class="container text-center"> <hr style="margin-top:0;margin-bottom:.3rem;"> <a href="https://creativecommons.org/licenses/by/4.0/" target="_blank" class="text-muted small">Creative Commons Attribution 4.0 International License</a> <div id="copy" class="mt-2">© 2024 World Academy of Science, Engineering and Technology</div> </div> </footer> <a href="javascript:" id="return-to-top"><i class="fas fa-arrow-up"></i></a> <div class="modal" id="modal-template"> <div class="modal-dialog"> <div class="modal-content"> <div class="row m-0 mt-1"> <div class="col-md-12"> <button type="button" class="close" data-dismiss="modal" aria-label="Close"><span aria-hidden="true">×</span></button> </div> </div> <div class="modal-body"></div> </div> </div> </div> <script src="https://cdn.waset.org/static/plugins/jquery-3.3.1.min.js"></script> <script src="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/js/bootstrap.bundle.min.js"></script> <script src="https://cdn.waset.org/static/js/site.js?v=150220211556"></script> <script> jQuery(document).ready(function() { /*jQuery.get("https://publications.waset.org/xhr/user-menu", function (response) { jQuery('#mainNavMenu').append(response); });*/ jQuery.get({ url: "https://publications.waset.org/xhr/user-menu", cache: false }).then(function(response){ jQuery('#mainNavMenu').append(response); }); }); </script> </body> </html>