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enzymes</title> <meta name="description" content="Search results for: immobilized enzymes"> <meta name="keywords" content="immobilized enzymes"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar navbar-expand-lg navbar-light"> <a class="navbar-brand" href="https://waset.org"> <img src="https://cdn.waset.org/static/images/wasetc.png" alt="Open Science Research Excellence" title="Open Science Research Excellence" /> </a> <button class="d-block d-lg-none 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action="https://publications.waset.org/abstracts/search"> <div id="custom-search-input"> <div class="input-group"> <i class="fas fa-search"></i> <input type="text" class="search-query" name="q" placeholder="Author, Title, Abstract, Keywords" value="immobilized enzymes"> <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> 828</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: immobilized enzymes</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">828</span> Improvement on the Specific Activities of Immobilized Enzymes by Poly(Ethylene Oxide) Surface Modification</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shaohua%20Li">Shaohua Li</a>, <a href="https://publications.waset.org/abstracts/search?q=Aihua%20Zhang"> Aihua Zhang</a>, <a href="https://publications.waset.org/abstracts/search?q=Kelly%20Zatopek"> Kelly Zatopek</a>, <a href="https://publications.waset.org/abstracts/search?q=Saba%20Parvez"> Saba Parvez</a>, <a href="https://publications.waset.org/abstracts/search?q=Andrew%20F.%20Gardner"> Andrew F. Gardner</a>, <a href="https://publications.waset.org/abstracts/search?q=Ivan%20R.%20Corr%C3%AAa%20Jr."> Ivan R. Corrêa Jr.</a>, <a href="https://publications.waset.org/abstracts/search?q=Christopher%20J.%20Noren"> Christopher J. Noren</a>, <a href="https://publications.waset.org/abstracts/search?q=Ming-Qun%20Xu"> Ming-Qun Xu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Covalent immobilization of enzymes on solid supports is an alternative approach to biocatalysis with the added benefits of simple enzyme removal, improved stability, and adaptability to automation and high-throughput applications. Nevertheless, immobilized enzymes generally suffer from reduced activities compared to their soluble counterparts. One major factor leading to activity loss is the intrinsic hydrophobic property of the supporting material surface, which could result in the conformational change/confinement of enzymes. We report a strategy of utilizing flexible poly (ethylene oxide) (PEO) moieties as to improve the surface hydrophilicity of solid supports used for enzyme immobilization. DNA modifying enzymes were covalently conjugated to PEO-coated magnetic-beads. Kinetics studies proved that the activities of the covalently-immobilized DNA modifying enzymes were greatly enhanced by the PEO modification on the bead surface. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=immobilized%20enzymes" title="immobilized enzymes">immobilized enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=biocatalysis" title=" biocatalysis"> biocatalysis</a>, <a href="https://publications.waset.org/abstracts/search?q=poly%28ethylene%20oxide%29" title=" poly(ethylene oxide)"> poly(ethylene oxide)</a>, <a href="https://publications.waset.org/abstracts/search?q=surface%20modification" title=" surface modification"> surface modification</a> </p> <a href="https://publications.waset.org/abstracts/79716/improvement-on-the-specific-activities-of-immobilized-enzymes-by-polyethylene-oxide-surface-modification" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/79716.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">308</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">827</span> A Novel Alginate/Tea Waste Complex for Restoration and Conservation of Historical Textiles Using Immobilized Enzymes</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohamed%20E.%20Hassan">Mohamed E. Hassan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Through numerous chemical linkages, historical textiles in burial contexts or in museums are exposed to many different forms of stains and filth. The cleaning procedure must be carried out carefully without causing any irreparable harm, and sediments must be removed without damaging the surface's original material. Science and technology continue to develop novel methods for cleaning historical textiles and artistic surfaces biologically (using enzymes). Lipase and α-amylase were immobilized on nanoparticles of alginate/tea waste nanoparticle complex and used in historical textile cleaning. The preparation of nanoparticles, activation, and enzyme immobilization were characterized. Optimization of loading times and units of the two enzymes was done. It was found that the optimum time and units of amylase were 3 hours and 30 U, respectively. While the optimum time and units of lipase were 2.5 hours and 20 U, respectively, FT-IR and TGA instruments were used in proving the preparation of nanoparticles and the immobilization process. SEM was used to examine the fibres before and after treatment. In conclusion, a new carrier was prepared from alginate/Tea waste and optimized to be used in the restoration and conservation of historical textiles using immobilized lipase and α-amylase. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alginate%2Ftea%20waste" title="alginate/tea waste">alginate/tea waste</a>, <a href="https://publications.waset.org/abstracts/search?q=nanoparticles" title=" nanoparticles"> nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilized%20enzymes" title=" immobilized enzymes"> immobilized enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=historical%20textiles" title=" historical textiles"> historical textiles</a> </p> <a href="https://publications.waset.org/abstracts/166235/a-novel-alginatetea-waste-complex-for-restoration-and-conservation-of-historical-textiles-using-immobilized-enzymes" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/166235.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">88</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">826</span> Restoration and Conservation of Historical Textiles Using Covalently Immobilized Enzymes on Nanoparticles</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohamed%20Elbehery">Mohamed Elbehery</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Historical textiles in the burial environment or in museums are exposed to many types of stains and dirt that are associated with historical textiles by multiple chemical bonds that cause damage to historical textiles. The cleaning process must be carried out with great care, with no irreversible damage, and sediments removed without affecting the original material of the surface being cleaned. Science and technology continue to provide innovative systems in the bio-cleaning process (using pure enzymes) of historical textiles and artistic surfaces. Lipase and α-amylase were immobilized on nanoparticles of alginate/κ-carrageenan nanoparticle complex and used in historical textiles cleaning. Preparation of nanoparticles, activation, and enzymes immobilization were characterized. Optimization of loading time and units of the two enzymes were done. It was found that, the optimum time and units of amylase were 4 hrs and 25U, respectively. While, the optimum time and units of lipase were 3 hrs and 15U, respectively. The methods used to examine the fibers using a scanning electron microscope equipped with an X-ray energy dispersal unit: SEM with EDX unit. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=nanoparticles" title="nanoparticles">nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=enzymes" title=" enzymes"> enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=textiles" title=" textiles"> textiles</a> </p> <a href="https://publications.waset.org/abstracts/166234/restoration-and-conservation-of-historical-textiles-using-covalently-immobilized-enzymes-on-nanoparticles" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/166234.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">99</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">825</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">387</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">824</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">823</span> Enhanced Enzymes Production through Immobilization of Filamentous Fungi</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Zhanara%20B.%20Suleimenova">Zhanara B. Suleimenova</a>, <a href="https://publications.waset.org/abstracts/search?q=Zhazira%20K.%20Saduyeva"> Zhazira K. Saduyeva</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Filamentous fungi are major producers of enzymes that have important applications in the food and beverage industries. The overall objective of this research is a strain improvement technology for efficient industrial enzymes production. The new way of filamentous fungi cultivation method has been developed. Such technology prolong producers’ cultivation period up to 60 days and create the opportunity to obtain enzymes repeatedly in every 2-3 days of fungal cultivation. This method is based on immobilizing enzymes producers with solid support in submerged conditions of growth. Immobilizing has a range of advantages: Decreasing the price of the final product, absence of foreign substances, controlled process of enzyme-genesis, ability of various enzymes simultaneous production, etc. Design of proposed technology gives the opportunity to increase the activity of immobilized cells culture filtrate comparing to free cells, growing in periodic culture conditions. Thus, proposed research focuses on new, more versatile, microorganisms capable of squeezing more end-products as well as proposed cultivation technology led to increased enzymatic productivity by several times. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=filamentous%20fungi" title="filamentous fungi">filamentous fungi</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%20enzymes%20production" title=" industrial enzymes production"> industrial enzymes production</a>, <a href="https://publications.waset.org/abstracts/search?q=strain%20improvement" title=" strain improvement "> strain improvement </a> </p> <a href="https://publications.waset.org/abstracts/27195/enhanced-enzymes-production-through-immobilization-of-filamentous-fungi" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/27195.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">359</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">822</span> Synthesis of DHA Rich Glycerides with Immobilized Lipases from Mucor miehei and Rhizopus oryzae </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Satyendra%20P.%20Chaurasia">Satyendra P. Chaurasia</a>, <a href="https://publications.waset.org/abstracts/search?q=Aditi%20Sharma"> Aditi Sharma</a>, <a href="https://publications.waset.org/abstracts/search?q=Ajay%20K.%20Dalai"> Ajay K. Dalai </a> </p> <p class="card-text"><strong>Abstract:</strong></p> The esterification of Docosahexaenoic acid (DHA) with glycerol using immobilized Mucor mie-hei lipase (MML) and Rhizopus oryzae lipase (ROL) have been studied in the present paper to synthesize triglycerides (TG) rich in DHA. Both immobilized lipases (MML and ROL), and their support materials (immobead-150 and ion-exchange resin) were characterized and compared for surface properties with BET, for chemical functional groups with FT-IR, and for particle size distribution with particle size analyzer. The most suitable reaction conditions for synthesis of DHA rich TG in biphasic solvent system were found as 1:3 (wt/wt) glycerol to DHA ratio, 1:1 (wt/wt) buffer to DHA ratio, 1:1 (wt/wt) solvent to DHA ratio at 50 ºC temperature, and 600 rpm speed of agitation with 100 mg of immobilized lipases. Maximum 95.9 % esterification was obtained with immobilized MML in 14 days reaction with formation of 65.7 wt% DHA rich TG. Whereas, immobilized ROL has shown formation of only 23.8 wt% DHA rich TG with total 78.9 % esterification in 15 days. Additionally, repeated use of both immobilized lipases was con-ducted up to five cycles, indicated 50.4% and 41.2 % activity retention after fifth repeated use of immobilized MML and ROL, respectively. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=DHA" title="DHA">DHA</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilized%20Mucor%20miehei%20lipase" title=" immobilized Mucor miehei lipase"> immobilized Mucor miehei lipase</a>, <a href="https://publications.waset.org/abstracts/search?q=Rhizopus%20oryzae%20lipase" title=" Rhizopus oryzae lipase"> Rhizopus oryzae lipase</a>, <a href="https://publications.waset.org/abstracts/search?q=esterification" title=" esterification"> esterification</a> </p> <a href="https://publications.waset.org/abstracts/30020/synthesis-of-dha-rich-glycerides-with-immobilized-lipases-from-mucor-miehei-and-rhizopus-oryzae" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/30020.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">353</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">821</span> Development of Strategy for Enhanced Production of Industrial Enzymes by Microscopic Fungi in Submerged Fermentation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Zhanara%20Suleimenova">Zhanara Suleimenova</a>, <a href="https://publications.waset.org/abstracts/search?q=Raushan%20Blieva"> Raushan Blieva</a>, <a href="https://publications.waset.org/abstracts/search?q=Aigerim%20Zhakipbekova"> Aigerim Zhakipbekova</a>, <a href="https://publications.waset.org/abstracts/search?q=Inkar%20Tapenbayeva"> Inkar Tapenbayeva</a>, <a href="https://publications.waset.org/abstracts/search?q=Zhanar%20Narmuratova"> Zhanar Narmuratova</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Green processes are based on innovative technologies that do not negatively affect the environment. Industrial enzymes originated from biological systems can effectively contribute to sustainable development through being isolated from microorganisms which are fermented using primarily renewable resources. Many widespread microorganisms secrete a significant amount of biocatalysts into the environment, which greatly facilitates the task of their isolation and purification. The ability to control the enzyme production through the regulation of their biosynthesis and the selection of nutrient media and cultivation conditions allows not only to increase the yield of enzymes but also to obtain enzymes with certain properties. In this regard, large potentialities are embedded in immobilized cells. Enzyme production technology in a secreted active form enabling industrial application on an economically feasible scale has been developed. This method is based on the immobilization of enzyme producers on a solid career. Immobilizing has a range of advantages: decreasing the price of the final product, absence of foreign substances, controlled process of enzyme-genesis, the ability of various enzymes' simultaneous production, etc. Design of proposed equipment gives the opportunity to increase the activity of immobilized cell culture filtrate comparing to free cells, growing in periodic culture conditions. Such technology allows giving a 10-times raise in culture productivity, to prolong the process of fungi cultivation and periods of active culture liquid generation. Also, it gives the way to improve the quality of filtrates (to make them more clear) and exclude time-consuming processes of recharging fermentative vials, that require manual removing of mycelium. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=industrial%20enzymes" title="industrial enzymes">industrial enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=submerged%20fermentation" title=" submerged fermentation"> submerged fermentation</a>, <a href="https://publications.waset.org/abstracts/search?q=microscopic%20fungi" title=" microscopic fungi"> microscopic fungi</a> </p> <a href="https://publications.waset.org/abstracts/105924/development-of-strategy-for-enhanced-production-of-industrial-enzymes-by-microscopic-fungi-in-submerged-fermentation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/105924.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">141</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">820</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">819</span> Isolation, Characterization, and Optimization of Immobilized L-Asparginase- Anticancer Enzyme from Aspergillus.Niger</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Supriya%20Chatla">Supriya Chatla</a>, <a href="https://publications.waset.org/abstracts/search?q=Anjana%20Male"> Anjana Male</a>, <a href="https://publications.waset.org/abstracts/search?q=Srikala%20Kamireddy"> Srikala Kamireddy</a> </p> <p class="card-text"><strong>Abstract:</strong></p> L-asparaginase (E.C.3.5.1.1) is an anti-cancer enzyme that has been purified and characterized for decades to study and evaluate its anti-carcinogenic activity against Hodgkin’s lymphoma. The present investigation deals with screening, isolation and optimization of L-asparaginase giving fungal strain of soil samples from different areas of AP, India. L-Aspariginase activity was estimated on the basis of the pink color surrounding the growing colony. A total of 132 colonies were screened and isolated from different samples. Based on the zone diameter, L-asparaginase activity is determined, L- asparaginase activity is optimized at 28oc and Immobilized Aspariginase had more potency than the free enzymes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aspariginase" title="aspariginase">aspariginase</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme" title=" anticancer enzyme"> anticancer enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=Isolation" title=" Isolation"> Isolation</a>, <a href="https://publications.waset.org/abstracts/search?q=optimization" title=" optimization"> optimization</a> </p> <a href="https://publications.waset.org/abstracts/161845/isolation-characterization-and-optimization-of-immobilized-l-asparginase-anticancer-enzyme-from-aspergillusniger" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/161845.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">80</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">818</span> Magnetite Nanoparticles Immobilized Pectinase: Preparation, Characterization and Application for the Fruit Juices Clarification</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Leila%20Mosafa">Leila Mosafa</a>, <a href="https://publications.waset.org/abstracts/search?q=Majid%20Moghadam"> Majid Moghadam</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohammad%20Shahedi"> Mohammad Shahedi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this work, pectinase was immobilized on the surface of silica-coated magnetite nanoparticles via covalent attachment. The magnetite-immobilized enzyme was characterized by Fourier transform infrared spectroscopy, X-ray powder diffraction, scanning electron microscopy and vibrating sample magnetometry techniques. Response surface methodology using Minitab Software was applied for statistical designing of operating conditions in order to immobilize pectinase on magnetic nanoparticles. The optimal conditions were obtained at 30°C and pH 5.5 with 42.97 µl pectinase for 2 h. The immobilization yield was 50.6% at optimized conditions. Compared to the free pectinase, the immobilized pectinase was found to exhibit enhanced enzyme activity, better tolerance to the variation of pH and temperature, and improved storage stability. Both free and immobilized samples reduced the viscosity of apple juice from 1.12 to 0.88 and 0.92 mm2s-1, respectively, after 30 min at their optimum temperature. Furthermore, the immobilized enzyme could be reused six consecutive cycles and the efficiency loss in viscosity reduction was found to be only 8.16%. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=magnetite%20nanoparticles" title="magnetite nanoparticles">magnetite nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=pectinase%20enzyme" title=" pectinase enzyme"> pectinase enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=juice%20clarification" title=" juice clarification"> juice clarification</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20activity" title=" enzyme activity "> enzyme activity </a> </p> <a href="https://publications.waset.org/abstracts/6143/magnetite-nanoparticles-immobilized-pectinase-preparation-characterization-and-application-for-the-fruit-juices-clarification" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/6143.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">407</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">817</span> Laccase Catalysed Conjugation of Tea Polyphenols for Enhanced Antioxidant Properties</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Parikshit%20Gogo">Parikshit Gogo</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20N.%20Dutta"> N. N. Dutta</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The oxidative enzymes specially laccase (benzenediol: oxygen oxidoreductase, E.C.1.10.3.2) from bacteria, fungi and plants have been playing an important role in green technologies due to their specific advantageous properties. Laccase from different sources and in different forms was used as a biocatalyst in many oxidation and conjugation reactions starting from phenol to hydrocarbons. Tea polyphenols and its derivatives attract the scientific community because of their potential use as antioxidants in food, pharmaceutical and cosmetic industries. Conjugate of polyphenols emerged as a novel materials which shows better stability and antioxidant properties in applied fields. The conjugation reaction of catechin with poly (allylamine) has been studied using free, immobilized and cross-linked enzyme crystals (CLEC) of laccase from Trametes versicolor with particular emphasis on the effect of pertinent variables and kinetic aspects of the reaction. The stability and antioxidant property of the conjugated product was improved as compared to the unconjugated tea polyphenols. The reaction was studied in 11 different solvents in order to deduce the solvent effect through an attempt to correlate the initial reaction rate with solvent properties such as hydrophobicity (logP), water solubility (logSw), electron pair acceptance (ETN) and donation abilities (DNN), polarisibility and dielectric constant which exhibit reasonable correlations. The study revealed, in general that polar solvents favour the initial reaction rate. The kinetics of the conjugation reaction conformed to the so-called Ping-Pong-Bi-Bi mechanism with catechin inhibition. The stability as well as activity of the CLEC was better than the free enzymes and immobilized laccase for practical application. In case of immobilized laccase system marginal diffusional limitation could be inferred from the experimental data. The kinetic parameters estimated by non-linear regression analysis were found to be KmPAA(mM) = 0.75, 1.8967 and Kmcat (mM) = 11.769, 15.1816 for free and immobilized laccase respectively. An attempt has been made to assess the activity of the laccase for the conjugation reaction in relation to other reactions such as dimerisation of ferulic acids and develop a protocol to enhance polyphenol antioxidant activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=laccase" title="laccase">laccase</a>, <a href="https://publications.waset.org/abstracts/search?q=catechin" title=" catechin"> catechin</a>, <a href="https://publications.waset.org/abstracts/search?q=conjugation%20reaction" title=" conjugation reaction"> conjugation reaction</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20properties" title=" antioxidant properties"> antioxidant properties</a> </p> <a href="https://publications.waset.org/abstracts/28634/laccase-catalysed-conjugation-of-tea-polyphenols-for-enhanced-antioxidant-properties" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/28634.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">270</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">816</span> Immobilization of Horseradish Peroxidase onto Bio-Linked Magnetic Particles with Allium Cepa Peel Water Extracts</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mirjana%20Petronijevi%C4%87">Mirjana Petronijević</a>, <a href="https://publications.waset.org/abstracts/search?q=Sanja%20Pani%C4%87"> Sanja Panić</a>, <a href="https://publications.waset.org/abstracts/search?q=Aleksandra%20Cvetanovi%C4%87"> Aleksandra Cvetanović</a>, <a href="https://publications.waset.org/abstracts/search?q=Branko%20Kordi%C4%87"> Branko Kordić</a>, <a href="https://publications.waset.org/abstracts/search?q=Nenad%20Grba"> Nenad Grba</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Enzyme peroxidases are biological catalysts and play a major role in phenolic wastewater treatments and other environmental applications. The most studied species from the peroxidases family is horseradish peroxidase (HRP). In environmental processes, HRP could be used in its free or immobilized form. Enzyme immobilization onto solid support is performed to improve the enzyme properties, prolong its lifespan and operational stability and allow its reuse in industrial applications. One of the enzyme supports of a newer generation is magnetic particles (MPs). Fe₃O₄ MPs are the most widely pursued immobilization of enzymes owing to their remarkable advantages of biocompatibility and non-toxicity. Also, MPs can be easily separated and recovered from the water by applying an external magnetic field. On the other hand, metals and metal oxides are not suitable for the covalent binding of enzymes, so it is necessary to perform their surface modification. Fe₃O₄ MPs functionalization could be performed during the process of their synthesis if it takes place in the presence of plant extracts. Extracts of plant material, such as wild plants, herbs, even waste materials of the food and agricultural industry (bark, shell, leaves, peel), are rich in various bioactive components such as polyphenols, flavonoids, sugars, etc. When the synthesis of magnetite is performed in the presence of plant extracts, bioactive components are incorporated into the surface of the magnetite, thereby affecting its functionalization. In this paper, the suitability of bio-magnetite as solid support for covalent immobilization of HRP across glutaraldehyde was examined. The activity of immobilized HRP at different pH values (4-9) and temperatures (20-80°C) and reusability were examined. Bio-MP was synthesized by co-precipitation method from Fe(II) and Fe(III) sulfate salts in the presence of water extract of the Allium cepa peel. The water extract showed 81% of antiradical potential (according to DPPH assay), which is connected with the high content of polyphenols. According to the FTIR analysis, the bio-magnetite contains oxygen functional groups (-OH, -COOH, C=O) suitable for binding to glutaraldehyde, after which the enzyme is covalently immobilized. The immobilized enzyme showed high activity at ambient temperature and pH 7 (30 U/g) and retained ≥ 80% of its activity at a wide range of pH (5-8) and temperature (20-50°C). The HRP immobilized onto bio-MPs showed remarkable stability towards temperature and pH variations compared to the free enzyme form. On the other hand, immobilized HRP showed low reusability after the first washing cycle enzyme retains 50% of its activity, while after the third washing cycle retains only 22%. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=bio-magnetite" title="bio-magnetite">bio-magnetite</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=water%20extracts" title=" water extracts"> water extracts</a>, <a href="https://publications.waset.org/abstracts/search?q=environmental%20protection" title=" environmental protection"> environmental protection</a> </p> <a href="https://publications.waset.org/abstracts/142934/immobilization-of-horseradish-peroxidase-onto-bio-linked-magnetic-particles-with-allium-cepa-peel-water-extracts" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/142934.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">223</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">815</span> Study on the Heavy Oil Degradation Performance and Kinetics of Immobilized Bacteria on Modified Zeolite</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Xiao%20L%20Dai">Xiao L Dai</a>, <a href="https://publications.waset.org/abstracts/search?q=Wen%20X%20Wei"> Wen X Wei</a>, <a href="https://publications.waset.org/abstracts/search?q=Shuo%20Wang"> Shuo Wang</a>, <a href="https://publications.waset.org/abstracts/search?q=Jia%20B%20Li"> Jia B Li</a>, <a href="https://publications.waset.org/abstracts/search?q=Yan%20Wei"> Yan Wei</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Heavy oil pollution generated from both natural and anthropogenic sources could cause significant damages to the ecological environment, due to the toxicity of some of its constituents. Nowadays, microbial remediation is becoming a promising technology to treat oil pollution owing to its low cost and prevention of secondary pollution; microorganisms are key players in the process. Compared to the free microorganisms, immobilized microorganisms possess several advantages, including high metabolic activity rates, strong resistance to toxic chemicals and natural competition with the indigenous microorganisms, and effective resistance to washing away (in open water system). Many immobilized microorganisms have been successfully used for bioremediation of heavy oil pollution. Considering the broad choices, low cost, simple process, large specific surface area and less impact on microbial activity, modified zeolite were selected as a bio-carrier for bacteria immobilization. Three strains of heavy oil-degrading bacteria Bacillus sp. DL-13, Brevibacillus sp. DL-1 and Acinetobacter sp. DL-34 were immobilized on the modified zeolite under mild conditions, and the bacterial load (bacteria /modified zeolite) was 1.12 mg/g, 1.11 mg/g, and 1.13 mg/g, respectively. SEM results showed that the bacteria mainly adsorbed on the surface or punctured in the void of modified zeolite. The heavy oil degradation efficiency of immobilized bacteria was 62.96%, higher than that of the free bacteria (59.83%). The heavy oil degradation process of immobilized bacteria accords with the first-order reaction equation, and the reaction rate constant is 0.1483 d⁻¹, which was significantly higher than the free bacteria (0.1123 d⁻¹), suggesting that the immobilized bacteria can rapidly start up the heavy oil degradation and has a high activity of heavy oil degradation. The results suggested that immobilized bacteria are promising technology for bioremediation of oil pollution. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=heavy%20oil%20pollution" title="heavy oil pollution">heavy oil pollution</a>, <a href="https://publications.waset.org/abstracts/search?q=microbial%20remediation" title=" microbial remediation"> microbial remediation</a>, <a href="https://publications.waset.org/abstracts/search?q=modified%20zeolite" title=" modified zeolite"> modified zeolite</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilized%20bacteria" title=" immobilized bacteria"> immobilized bacteria</a> </p> <a href="https://publications.waset.org/abstracts/110195/study-on-the-heavy-oil-degradation-performance-and-kinetics-of-immobilized-bacteria-on-modified-zeolite" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/110195.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">814</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">813</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">812</span> Different Formula of Mixed Bacteria as a Bio-Treatment for Sewage Wastewater</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=E.%20Marei">E. Marei</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Hammad"> A. Hammad</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20Ismail"> S. Ismail</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20El-Gindy"> A. El-Gindy</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study aims to investigate the ability of different formula of mixed bacteria as a biological treatments of wastewater after primary treatment as a bio-treatment and bio-removal and bio-adsorbent of different heavy metals in natural circumstances. The wastewater was collected from Sarpium forest site-Ismailia Governorate, Egypt. These treatments were mixture of free cells and mixture of immobilized cells of different bacteria. These different formulas of mixed bacteria were prepared under Lab. condition. The obtained data indicated that, as a result of wastewater bio-treatment, the removal rate was found to be 76.92 and 76.70% for biological oxygen demand, 79.78 and 71.07% for chemical oxygen demand, 32.45 and 36.84 % for ammonia nitrogen as well as 91.67 and 50.0% for phosphate after 24 and 28 hrs with mixed free cells and mixed immobilized cells, respectively. Moreover, the bio-removals of different heavy metals were found to reach 90.0 and 50. 0% for Cu ion, 98.0 and 98.5% for Fe ion, 97.0 and 99.3% for Mn ion, 90.0 and 90.0% Pb, 80.0% and 75.0% for Zn ion after 24 and 28 hrs with mixed free cells and mixed immobilized cells, respectively. The results indicated that 13.86 and 17.43% of removal efficiency and reduction of total dissolved solids were achieved after 24 and 28 hrs with mixed free cells and mixed immobilized cells, respectively. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=wastewater%20%20bio-treatment" title="wastewater bio-treatment ">wastewater bio-treatment </a>, <a href="https://publications.waset.org/abstracts/search?q=bio-sorption%20heavy%20metals" title=" bio-sorption heavy metals"> bio-sorption heavy metals</a>, <a href="https://publications.waset.org/abstracts/search?q=biological%20desalination" title=" biological desalination"> biological desalination</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilized%20bacteria" title=" immobilized bacteria"> immobilized bacteria</a>, <a href="https://publications.waset.org/abstracts/search?q=free%20cell%20bacteria" title=" free cell bacteria"> free cell bacteria</a> </p> <a href="https://publications.waset.org/abstracts/88568/different-formula-of-mixed-bacteria-as-a-bio-treatment-for-sewage-wastewater" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/88568.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">201</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">811</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">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">810</span> Development of Enzymatic Amperometric Biosensors with Carbon Nanotubes Decorated with Iron Oxide Nanoparticles</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Uc-Cayetano%20E.%20G.">Uc-Cayetano E. G.</a>, <a href="https://publications.waset.org/abstracts/search?q=Ake-Uh%20O.%20E."> Ake-Uh O. E.</a>, <a href="https://publications.waset.org/abstracts/search?q=Villanueva-Mena%20I.%20E."> Villanueva-Mena I. E.</a>, <a href="https://publications.waset.org/abstracts/search?q=Ordonez%20L.%20C."> Ordonez L. C.</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Carbon nanotubes (CNTs) and other graphitic nanostructures are materials with extraordinary physical, physicochemical and electrochemical properties which are being aggressively investigated for a variety of sensing applications. Thus, sensing of biological molecules such as proteins, DNA, glucose and other enzymes using either single wall or multiwall carbon nanotubes (MWCNTs) has been widely reported. Despite the current progress in this area, the electrochemical response of CNTs used in a variety of sensing arrangements still needs to be improved. An alternative towards the enhancement of this CNTs' electrochemical response is to chemically (or physically) modify its surface. The influence of the decoration with iron oxide nanoparticles in different types of MWCNTs on the amperometric sensing of glucose, urea, and cholesterol in solution is investigated. Commercial MWCNTs were oxidized in acid media and subsequently decorated with iron oxide nanoparticles; finally, the enzymes glucose oxidase, urease, and cholesterol oxidase are chemically immobilized to oxidized and decorated MWCNTs for glucose, urease, and cholesterol electrochemical sensing. The results of the electrochemical characterizations consistently show that the presence of iron oxide nanoparticles decorating the surface of MWCNTs enhance the amperometric response and the sensitivity to increments in glucose, urease, and cholesterol concentration when compared to non-decorated MWCNTs. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=WCNTs" title="WCNTs">WCNTs</a>, <a href="https://publications.waset.org/abstracts/search?q=enzymes" title=" enzymes"> enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=oxidation" title=" oxidation"> oxidation</a>, <a href="https://publications.waset.org/abstracts/search?q=decoration" title=" decoration"> decoration</a> </p> <a href="https://publications.waset.org/abstracts/106360/development-of-enzymatic-amperometric-biosensors-with-carbon-nanotubes-decorated-with-iron-oxide-nanoparticles" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/106360.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">129</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">809</span> Eradication of Gram-Positive Bacteria by Photosensitizers Immobilized in Polymers </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Marina%20Nisnevitch">Marina Nisnevitch</a>, <a href="https://publications.waset.org/abstracts/search?q=Anton%20Valkov"> Anton Valkov</a>, <a href="https://publications.waset.org/abstracts/search?q=Faina%20Nakonechny"> Faina Nakonechny</a>, <a href="https://publications.waset.org/abstracts/search?q=Kate%20Adar%20Raik"> Kate Adar Raik</a>, <a href="https://publications.waset.org/abstracts/search?q=Yamit%20Mualem"> Yamit Mualem</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Photosensitizers are dye compounds belonging to various chemical groups that in all the cases have a developed structure of conjugated double bonds. Under illumination with visible light, the photosensitizers are excited and transfer the absorbed energy to the oxygen dissolved in an aqueous phase, leading to production of a reactive oxygen species which cause irreversible damage to bacterial cells. When immobilized onto a solid phase, photosensitizers preserve their antibacterial properties. In the present study, photosensitizers were immobilized in polyethylene or propylene and tested for antimicrobial activity against Gram-positive S. aureus, S. epidermidis and Streptococcus sp. For this purpose, water-soluble photosensitizers, Rose Bengal sodium salt, and methylene blue as well as water-insoluble hematoporphyrin and Rose Bengal lactone, were immobilized by dissolution in melted polymers to yield 3 mm diameter rods and 3-5 mm beads. All four photosensitizers were found to be effective in the eradication of Gram-positive bacteria under illumination by a white luminescent lamp or sunlight. The immobilized photosensitizers can be applied for continuous water disinfection; they can be easily removed at the end of the treatment and reused. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=antimicrobial%20polymers" title="antimicrobial polymers">antimicrobial polymers</a>, <a href="https://publications.waset.org/abstracts/search?q=gram-positive%20bacteria" title=" gram-positive bacteria"> gram-positive bacteria</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization%20of%20photosensitizers" title=" immobilization of photosensitizers"> immobilization of photosensitizers</a>, <a href="https://publications.waset.org/abstracts/search?q=photodynamic%20antibacterial%20activity" title=" photodynamic antibacterial activity"> photodynamic antibacterial activity</a> </p> <a href="https://publications.waset.org/abstracts/46641/eradication-of-gram-positive-bacteria-by-photosensitizers-immobilized-in-polymers" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/46641.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">241</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">808</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">807</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">806</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">805</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">804</span> Encapsulated Rennin Enzyme in Nano and Micro Tubular Cellulose/Starch Gel Composite for Milk Coagulation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Eleftheria%20Barouni">Eleftheria Barouni</a>, <a href="https://publications.waset.org/abstracts/search?q=Theano%20Petsi"> Theano Petsi</a>, <a href="https://publications.waset.org/abstracts/search?q=Argyro%20Bekatorou"> Argyro Bekatorou</a>, <a href="https://publications.waset.org/abstracts/search?q=Dionysos%20Kolliopoulos"> Dionysos Kolliopoulos</a>, <a href="https://publications.waset.org/abstracts/search?q=Dimitrios%20Vasileiou"> Dimitrios Vasileiou</a>, <a href="https://publications.waset.org/abstracts/search?q=Panayiotis%20Panas"> Panayiotis Panas</a>, <a href="https://publications.waset.org/abstracts/search?q=Maria%20Kanellaki"> Maria Kanellaki</a>, <a href="https://publications.waset.org/abstracts/search?q=Athanasios%20A.%20Koutinas"> Athanasios A. Koutinas</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The aim of the present work was the production and use of a composite filter (TC/starch), containing rennin enzyme, in continuous system and in successive fermentation batches (SFB) for milk coagulation in order to compare the operational stability of both systems and cheese production cost. Tubular cellulose (TC) was produced after removal of lignin from lignocellulosic biomass using several procedures, e.g. alkaline treatment [1] and starch gel was added for the reduction of TC tubes dimensions to micro- and nano- range[2]. Four immobilized biocatalysts were prepared using different ways of the enzyme entrapment. 1) TC/ rennin (rennin entrapped in the tubes of TC), 2) TC/SG-rennin (rennin entrapped in the tubes of the composite), 3) TC-SG/rennin (rennin entrapped into the layer of starch gel) and 4) TC/rennin- SG/rennin (rennin is entrapped both in the tubes of the TC and into the layer of starch gel). Firstly these immobilized biocatalysts were examined in ten SFB regarding the coagulation time and their activity All the above immobilized biocatalysts remained active and the coagulation time was ranged from 90 to 480, 120-480, 330-510, and 270-540 min for (1), (2), (3), and (4) respectively. The quality of the cheese was examined through the determination of volatile compounds by SPME GC/MS analysis. These results encouraged us to study a continuous coagulation system of milk. Even though the (1) immobilized biocatalyst gave lower coagulation time, we used the (2) immobilized biocatalyst in the continuous system. The results were promising. <p class="card-text"><strong>Keywords:</strong> <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=starch%20gel" title="starch gel">starch gel</a>, <a href="https://publications.waset.org/abstracts/search?q=composite%20biocatalyst" title=" composite biocatalyst"> composite biocatalyst</a>, <a href="https://publications.waset.org/abstracts/search?q=Rennin" title=" Rennin"> Rennin</a>, <a href="https://publications.waset.org/abstracts/search?q=milk%20coagulation" title=" milk coagulation"> milk coagulation</a> </p> <a href="https://publications.waset.org/abstracts/20843/encapsulated-rennin-enzyme-in-nano-and-micro-tubular-cellulosestarch-gel-composite-for-milk-coagulation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/20843.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">326</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">803</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">802</span> Effect of Non-Regulated pH on the Dynamics of Dark Fermentative Biohydrogen Production with Suspended and Immobilized Cell Culture </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Joelle%20Penniston">Joelle Penniston</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20B.%20Gueguim-Kana"> E. B. Gueguim-Kana </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Biohydrogen has been identified as a promising alternative to the use of non-renewable fossil reserves, owing to its sustainability and non-polluting nature. pH is considered as a key parameter in fermentative biohydrogen production processes, due to its effect on the hydrogenase activity, metabolic activity as well as substrate hydrolysis. The present study assesses the influence of regulating pH on dark fermentative biohydrogen production. Four experimental hydrogen production schemes were evaluated. Two were implemented using suspended cells under regulated pH growth conditions (Sus_R) and suspended and non-regulated pH (Sus_N). The two others regimes consisted of alginate immobilized cells under pH regulated growth conditions (Imm_R) and immobilized and non-pH regulated conditions (Imm_N). All experiments were carried out at 37.5°C with glucose as sole source of carbon. Sus_R showed a lag time of 5 hours and a peak hydrogen fraction of 36% and a glucose degradation of 37%, compared to Sus_N which showed a peak hydrogen fraction of 44% and complete glucose degradation. Both suspended culture systems showed a higher peak biohydrogen fraction compared to the immobilized cell system. Imm_R experiments showed a lag phase of 8 hours, a peak biohydrogen fraction of 35%, while Imm_N showed a lag phase of 5 hours, a peak biohydrogen fraction of 22%. 100% glucose degradation was observed in both pH regulated and non-regulated processes. This study showed that biohydrogen production in batch mode with suspended cells in a non-regulated pH environment results in a partial degradation of substrate, with lower yield. This scheme has been the culture mode of choice for most reported studies in biohydrogen research. The relatively lower slope in pH trend of the non-regulated pH experiment with immobilized cells (Imm_N) compared to Sus_N revealed that that immobilized systems have a better buffering capacity compared to suspended systems, which allows for the extended production of biohydrogen even under non-regulated pH conditions. However, alginate immobilized cultures in flask systems showed some drawbacks associated to high rate of gas production that leads to increased buoyancy of the immobilization beads. This ultimately impedes the release of gas out of the flask. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biohydrogen" title="biohydrogen">biohydrogen</a>, <a href="https://publications.waset.org/abstracts/search?q=sustainability" title=" sustainability"> sustainability</a>, <a href="https://publications.waset.org/abstracts/search?q=suspended" title=" suspended"> suspended</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilized" title=" immobilized "> immobilized </a> </p> <a href="https://publications.waset.org/abstracts/40020/effect-of-non-regulated-ph-on-the-dynamics-of-dark-fermentative-biohydrogen-production-with-suspended-and-immobilized-cell-culture" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/40020.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">801</span> Bacteria Immobilized Electrospun Fibrous Biocomposites for Cr (VI) Remediation in Water</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Omer%20Faruk%20Sarioglu">Omer Faruk Sarioglu</a>, <a href="https://publications.waset.org/abstracts/search?q=Asli%20Celebioglu"> Asli Celebioglu</a>, <a href="https://publications.waset.org/abstracts/search?q=Turgay%20Tekinay"> Turgay Tekinay</a>, <a href="https://publications.waset.org/abstracts/search?q=Tamer%20Uyar"> Tamer Uyar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Fibrous biocomposites were developed by immobilization of a Cr(VI) reducing bacterial strain, morganella morganii STB5, on electrospun polystyrene (PS) and polysulfone (PSU) webs. Cr(VI) removal characteristics of STB5/PS and STB5/PSU fibrous biocomposites were determined at 25 mg L-1 of initial Cr(VI) and 70.41% and 68.27% of removal were observed within 72 h, respectively. Reusability test results indicate that both biocomposites are potentially reusable and can be used for at least 5 cycles. After storage test results suggest that the biocomposites can be stored awhile without losing their Cr(VI) bioremoval capabilities. SEM images of STB5 immobilized PS and PSU webs after the reusability test exhibit strong attachment of bacterial biofilms onto fibrous surfaces. Our results are quite promising and suggesting that reusable bacteria immobilized electrospun fibrous biocomposites might be applicable for Cr(VI) remediation in water systems. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=electrospinning" title="electrospinning">electrospinning</a>, <a href="https://publications.waset.org/abstracts/search?q=polystyrene" title=" polystyrene"> polystyrene</a>, <a href="https://publications.waset.org/abstracts/search?q=polysulfone" title=" polysulfone"> polysulfone</a>, <a href="https://publications.waset.org/abstracts/search?q=Cr%28VI%29%20bioremoval" title=" Cr(VI) bioremoval"> Cr(VI) bioremoval</a>, <a href="https://publications.waset.org/abstracts/search?q=environmental%20sustainability" title=" environmental sustainability"> environmental sustainability</a> </p> <a href="https://publications.waset.org/abstracts/25210/bacteria-immobilized-electrospun-fibrous-biocomposites-for-cr-vi-remediation-in-water" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/25210.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">561</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">800</span> Biodegradation of Chlorpyrifos in Real Wastewater by Acromobacter xylosoxidans SRK5 Immobilized in Calcium Alginate</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Saira%20Khalid">Saira Khalid</a>, <a href="https://publications.waset.org/abstracts/search?q=Imran%20Hashmi"> Imran Hashmi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Agrochemical industries produce huge amount of wastewater containing pesticides and other harmful residues. Environmental regulations make it compulsory to bring pesticides to a minimum level before releasing wastewater from industrial units.The present study was designed with the objective to investigate biodegradation of CP in real wastewater using bacterial cells immobilized in calcium alginate. Bacterial strain identified as Acromobacter xylosoxidans SRK5 (KT013092) using 16S rRNA nucleotide sequence analysis was used. SRK5 was immobilized in calcium alginate to make calcium alginate microspheres (CAMs). Real wastewater from industry having 50 mg L⁻¹ of CP was inoculated with free cells or CAMs and incubated for 96 h at 37˚C. CP removal efficiency with CAMs was 98% after 72 h of incubation, and no lag phase was observed. With free cells, 12h of lag phase was observed. After 96 h of incubation 87% of CP removal was observed when inoculated with free cells. No adsorption was observed on vacant CAMs. Phytotoxicity assay demonstrated considerable loss in toxicity. Almost complete COD removal was achieved at 96 h with CAMs. Study suggests the use of immobilized cells of SRK5 for bioaugmentation of industrial wastewater for CP degradation instead of free cells. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biodegradation" title="biodegradation">biodegradation</a>, <a href="https://publications.waset.org/abstracts/search?q=chlorpyrifos" title=" chlorpyrifos"> chlorpyrifos</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=wastewater" title=" wastewater"> wastewater</a> </p> <a href="https://publications.waset.org/abstracts/93028/biodegradation-of-chlorpyrifos-in-real-wastewater-by-acromobacter-xylosoxidans-srk5-immobilized-in-calcium-alginate" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/93028.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">177</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">799</span> Formulation and Characterization of NaCS-PDMDAAC Capsules with Immobilized Chlorella vulgaris for Phycoremediation of 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=Quin%20Emparan">Quin Emparan</a>, <a href="https://publications.waset.org/abstracts/search?q=Razif%20Harun"> Razif Harun</a>, <a href="https://publications.waset.org/abstracts/search?q=Dayang%20R.%20A.%20Biak"> Dayang R. A. Biak</a>, <a href="https://publications.waset.org/abstracts/search?q=Rozita%20Omar"> Rozita Omar</a>, <a href="https://publications.waset.org/abstracts/search?q=Michael%20K.%20Danquah"> Michael K. Danquah</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cultivation of immobilized microalgae cells is on the rise for biotechnological applications. In this study, cultivation of Chlorella vulgaris was carried out in the form of suspended free-cell and immobilized cells system. NaCS-PDMDAAC capsules were used to immobilize C. vulgaris. Initially, the synthesized NaCS with C. vulgaris culture were prepared at various concentration of 5- 20% (w/v) using a 6% hardening solution (PDMDAAC) to investigate the capsules' gel stability and suitability for microalgae cells growth. Then, the capsules produced from 15% NaCS with C. vulgaris culture were furthered investigated using 5%, 10%, and 15% (w/v) of PDMDAAC solution. The capsules' gel stability was evaluated through dissolution time and loss of uniform spherical shape of capsules, while suitability for microalgae cells growth was evaluated through the optical density of microalgae. In this study, the 15% NaCS-10% PDMDAAC capsules were found to be the most suitable to sustain the capsules' gel stability and microalgae cells growth in MLA. For that reason, the C. vulgaris immobilized in the 15% NaCS-10% PDMDAAC capsules were further characterized using physicochemical analysis in terms of morphological, carbon (C), hydrogen (H) and nitrogen (N), Fourier transform-infrared (FT-IR), scanning electron microscopy-energy dispersive X-ray (SEM-EDX), zeta potential and Brunauer-Emmet-Teller (BET) analyses. The results revealed that the presence of sulfonates in the synthesized NaCS and NaCS-PDMDAAC capsules without and with C. vulgaris proves that cellulose alcohol group was successfully bonded by sulfo group. Besides that, immobilized microalgae cells have a smaller cell size of 6.29 ± 1.09 µm and zeta potential of -11.93 ± 0.91 mV than suspended free-cells microalgae culture. It can be summarized that immobilization of C. vulgaris in the 15% NaCS-10% PDMDAAC capsules are relevant as a bioremediator for wastewater treatment purposes due to its suitable size of pore and capsules as well as structural and compositional properties. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biological%20capsules" title="biological capsules">biological capsules</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilized%20cultivation" title=" immobilized cultivation"> immobilized cultivation</a>, <a href="https://publications.waset.org/abstracts/search?q=microalgae" title=" microalgae"> microalgae</a>, <a href="https://publications.waset.org/abstracts/search?q=physico-chemical%20analysis" title=" physico-chemical analysis"> physico-chemical analysis</a> </p> <a href="https://publications.waset.org/abstracts/104948/formulation-and-characterization-of-nacs-pdmdaac-capsules-with-immobilized-chlorella-vulgaris-for-phycoremediation-of-palm-oil-mill-effluent" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/104948.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">172</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=immobilized%20enzymes&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=immobilized%20enzymes&page=3">3</a></li> <li class="page-item"><a class="page-link" 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