Relevant bibliographies by topics / Enzyme entrapment

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Enzyme entrapment'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Enzyme entrapment"

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Sharma, Manu, Vinay Sharma та Dipak K. Majumdar. "Entrapment of α-Amylase in Agar Beads for Biocatalysis of Macromolecular Substrate". International Scholarly Research Notices 2014 (15 вересня 2014): 1–8. http://dx.doi.org/10.1155/2014/936129.

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Attempts have been made to optimize immobilization parameters, catalytic property, and stability of immobilized α-amylase in agar. The work compares natural entrapment efficiency of agar with the ionotropically cross-linked agar hydrogel, with the advantage of easy scale-up and cost and time effectiveness. Beads prepared with 3% (w/v) agar and 75 mM calcium chloride and hardened for 20 minutes were selected for further studies on the basis of entrapment efficiency (80%) and physical stability. Following entrapment, pH and temperature optima of enzyme were shifted from 6 to 6.5 and 50 to 55°C,
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Falcone, Shao, Rashid, and Kraatz. "Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels." Molecules 24, no. 16 (2019): 2884. http://dx.doi.org/10.3390/molecules24162884.

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Supramolecular amino acid and peptide hydrogels are functional materials with a wide range of applications, however, their ability to serve as matrices for enzyme entrapment have been rarely explored. Two amino acid conjugates were synthesized and explored for hydrogel formation. These hydrogels were characterized in terms of strength and morphology, and their ability to entrap enzymes while keeping them active and reusable was explored. It was found that the hydrogels were able to successfully entrap two common and significant enzymes—horseradish peroxidase and -amylase—thus keeping them act
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Imam, Hasan T., Patricia C. Marr, and Andrew C. Marr. "Enzyme entrapment, biocatalyst immobilization without covalent attachment." Green Chemistry 23, no. 14 (2021): 4980–5005. http://dx.doi.org/10.1039/d1gc01852c.

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Vlad-Oros, B., G. Preda, Z. Dudas, M. Dragomirescu, and A. Chiriac. "Entrapment of glucoamylase by sol-gel technique in PhTES/TEOS hybrid matrixes." Processing and Application of Ceramics 1, no. 1-2 (2007): 63–67. http://dx.doi.org/10.2298/pac0702063v.

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Mesoporous silica particles were prepared by the sol-gel method from different alkoxysilane precursors and used as a host matrix for encapsulation of glucoamylase, an enzyme widely used in fermentative industry. The aim was to investigate the physico-chemical properties of the different silica powders and their effect on the enzyme kinetics. The encapsulated enzymes followed Michaelis-Menten kinetics. The Michaelis constant (KM) and the maximum rate of starch hydrolysis reaction (Vmax) were calculated according to the Michaelis-Menten and Lineweaver-Burke plots. The values of the Michaelis con
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Le, Tuan, Selina Chan, Bassem Ebaid, and Monika Sommerhalter. "Silica Sol-Gel Entrapment of the Enzyme Chloroperoxidase." Journal of Nanotechnology 2015 (2015): 1–10. http://dx.doi.org/10.1155/2015/632076.

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The enzyme chloroperoxidase (CPO) was immobilized in silica sol-gel beads prepared from tetramethoxysilane. The average pore diameter of the silica host structure (~3 nm) was smaller than the globular CPO diameter (~6 nm) and the enzyme remained entrapped after sol-gel maturation. The catalytic performance of the entrapped enzyme was assessed via the pyrogallol peroxidation reaction. Sol-gel beads loaded with 4 μg CPO per mL sol solution reached 9–12% relative activity compared to free CPO in solution. Enzyme kinetic analysis revealed a decrease inkcatbut no changes inKMorKI. Product release o
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Han, Yu, Su Seong Lee, and Jackie Y. Ying. "Pressure-Driven Enzyme Entrapment in Siliceous Mesocellular Foam." Chemistry of Materials 18, no. 3 (2006): 643–49. http://dx.doi.org/10.1021/cm0520618.

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Heater, Bradley S., Zaofeng Yang, Marianne M. Lee, and Michael K. Chan. "In Vivo Enzyme Entrapment in a Protein Crystal." Journal of the American Chemical Society 142, no. 22 (2020): 9879–83. http://dx.doi.org/10.1021/jacs.9b13462.

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Nemzer, Louis R., Austin Schwartz, and A. J. Epstein. "Enzyme Entrapment in Reprecipitated Polyaniline Nano- and Microparticles." Macromolecules 43, no. 9 (2010): 4324–30. http://dx.doi.org/10.1021/ma100112g.

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Kowalski, Ann E., Lucas B. Johnson, Holly K. Dierl, Sehoo Park, Thaddaus R. Huber, and Christopher D. Snow. "Porous protein crystals as scaffolds for enzyme immobilization." Biomaterials Science 7, no. 5 (2019): 1898–904. http://dx.doi.org/10.1039/c8bm01378k.

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Wijayati, Nanik, Siti Anisa Rohmah, and Supartono Supartono. "SINTESIS ESTER-C SEBAGAI SENYAWA ANTIOKSIDAN MENGGUNAKAN BIOKATALIS ENZIM LIPASE/ZEOLIT ALAM." Jurnal Kimia Riset 1, no. 1 (2016): 7. http://dx.doi.org/10.20473/jkr.v1i1.2432.

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AbstrakImobilisasi enzim lipase merupakan metode yang digunakan untuk meningkatan daya tahan enzim terhadap perubahan lingkungan dan penggunaan secara berulang. Penelitian mengenai imobilisasi enzim lipase dari jamur tiram putih (Pleurotus ostreatus) telah dilakukan dengan metode entrapment (penjebakan, penjeratan) menggunakan zeolit alam teraktivasi dan larutan gel NaF. Waktu pengadukan optimum yang diperoleh dalam imobilisasi enzim lipase ialah selama 3 jam dengan nilai aktivitas lipase sebesar 4,24 U/mL dan enzim loading sebesar 63,07%. Enzim lipase terimobilisasi yang diperoleh diaplikasik
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Dissertations / Theses on the topic "Enzyme entrapment"

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Shenton, Daniel Paul. "New enzyme entrapment stabilisation using polymers." Thesis, University of Strathclyde, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249012.

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Hancock, James. "Organic Phase Entrapment of Glucose Oxidase In Polymeric Nanoparticles." University of Akron / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=akron1207860116.

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West, Jay M. "Probing the Mechanism of the Allosteric Transition of Aspartate Transcarbamoylase via Fluorescence, Physical Entrapment, and Small-Angle X-Ray Scattering." Thesis, Boston College, 2009. http://hdl.handle.net/2345/1356.

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Thesis advisor: Evan R. Kantrowitz<br>The regulatory mechanism of allostery is exhibited by certain proteins such as Escherichia coli aspartate transcarbamoylase (ATCase), and is defined as the change in shape and activity (of enzymes) resulting from the binding of particular molecules at locations distant from the active site. This particular enzyme and the property of allostery in general have been investigated for several decades, yet the molecular mechanisms underlying allosteric regulation remain unclear. Therefore in this thesis we have attempted via several biophysical methods, along wi
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Fagundes, Fabio Pereira. "Estudo da imobiliza??o de proteases para a s?ntese de oligolisinas." Universidade Federal do Rio Grande do Norte, 2011. http://repositorio.ufrn.br:8080/jspui/handle/123456789/17750.

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Made available in DSpace on 2014-12-17T15:42:15Z (GMT). No. of bitstreams: 1 FabioPF_TESE.pdf: 3376603 bytes, checksum: 15dfaa7fe12ca918fd7e1b98c4378dd9 (MD5) Previous issue date: 2011-09-16<br>Conselho Nacional de Desenvolvimento Cient?fico e Tecnol?gico<br>Enzymatic synthesis of peptides using proteases has attracted a great deal of attention in recent years. One key challenge in peptide synthesis is to find supports for protease immobilization capable of working in aqueous medium at high performance, producing watersoluble oligopeptides. At present, few reports have been described using t
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Lee, Yao-Wen, and 李耀文. "Metal-Nucleotide Hydrogel Entrapment and Cellulose Nanocrystal on Magnetic Alginate Microbeads for Enzyme Affinity Immobilization." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/3cd887.

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碩士<br>國立臺灣科技大學<br>化學工程系<br>106<br>In recent years, the amount of global diabetic patients increases. Diabetes can cause significant harm to human body, therefore it is very important to monitor blood sugar in diabetic patient. HbA1c is a product of glucose attached to the amino group of the N-terminal of hemoglobin β chain, which reflects long-term glycemic status of diabetic patients. In this study, fructosyl valine (FV), a simulated fragment of HbA1c will be oxidized by fructosyl peptide oxidase (FPO), that produces hydrogen peroxide (H2O2), and furthermore, color change will be developed wh
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Munauwarah, Rauzah, and 拉真. "Enzyme Immobilization on Carbon Paper Electrode Using Covalent-entrapment with Polypyrrole in Enzymatic Biofuel Cells." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/52520144055579173678.

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碩士<br>元智大學<br>化學工程與材料科學學系<br>104<br>Abstract Enzymatic biofuel cell is a subclass of biofuel cells that have application for low power devices (micro- to milliWatt). The working principle of enzymatic biofuel cell is employing enzymes as bioelectrocatalysts converting chemical energy to electrical energy, instead of metallic catalysts. This research aims to improve the immobilization method of electrodes to increase electrical power and life span from enzymatic biofuel cell using glucose oxidase in bio-anode, laccase in bio-cathode and glucose as the fuel. Both of these enzymes are immobilized
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CAI, XIU-YU, and 蔡修裕. "Characterization and inhibition study for naringinase from different sources and the immobilized enzyme with fiber entrapment method." Thesis, 1987. http://ndltd.ncl.edu.tw/handle/30927149265647415214.

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Book chapters on the topic "Enzyme entrapment"

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David, Allan E., Arthur J. Yang, and Nam Sun Wang. "Enzyme Stabilization and Immobilization by Sol-Gel Entrapment." In Enzyme Stabilization and Immobilization. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-895-9_6.

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Sassolas, Audrey, Akhtar Hayat, and Jean-Louis Marty. "Enzyme Immobilization by Entrapment Within a Gel Network." In Methods in Molecular Biology. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-550-7_15.

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Lowe, C. R., N. C. Foulds, S. E. Evans, and B. F. Y. Yon Hin. "Enzyme Entrapment in Conducting Organic Polymers: Application in Amperometric Biosensors." In Springer Series in Solid-State Sciences. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-83833-0_78.

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Madamwar, D., and K. Soni. "Biocatalysis in Non-Conventional Media by Entrapment of the Enzyme in Water-Restricted Microenvironment." In New Horizons in Biotechnology. Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0203-4_10.

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Buthe, Andreas. "Entrapment of Enzymes in Nanoporous Sol–Gels." In Methods in Molecular Biology. Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-132-1_18.

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Schlieker, Marc, and Klaus-Dieter Vorlop. "A Novel Immobilization Method for Entrapment: LentiKats®." In Immobilization of Enzymes and Cells. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-053-9_29.

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Fathi, Milad, Mehri Karim, Soroush Rahimi Khoigani, and Vahid Mosayebi. "Use of Nanotechnology for Immobilization and Entrapment of Food Applicable Enzymes." In Bioactive Molecules in Food. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-78030-6_52.

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Klyachko, Natalia L., and Andrey V. Levashov. "Surfactant Aggregates as Matrix Nanocontainers for Proteins (Enzymes) Entrapment and Regulation." In ACS Symposium Series. American Chemical Society, 2008. http://dx.doi.org/10.1021/bk-2008-0986.ch009.

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Fathi, Milad, Mehri Karim, Soroush Rahimi Khoigani, and Vahid Mosayebi. "Use of Nanotechnology for Immobilization and Entrapment of Food Applicable Enzymes." In Reference Series in Phytochemistry. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-54528-8_52-1.

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Fortier, Guy, Jian Wei Chen, and Daniel Bélanger. "Biosensors Based on Entrapment of Enzymes in a Water-Dispersed Anionic Polymer." In ACS Symposium Series. American Chemical Society, 1992. http://dx.doi.org/10.1021/bk-1992-0487.ch003.

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Conference papers on the topic "Enzyme entrapment"

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Alhajeri, Mubarak Muhammad, Jenn-Tai Liang, and Reza Barati Ghahfarokhi. "Polyelectrolyte Multilayered Nanoparticles as Nanocontainers for Enzyme Breakers During Hydraulic Fracturing Process." In SPE Annual Technical Conference and Exhibition. SPE, 2021. http://dx.doi.org/10.2118/205981-ms.

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Abstract In this study, Layer-by-Layer (LbL) assembled polyelectrolyte multilayered nanoparticles were developed as a technique for targeted and controlled release of enzyme breakers. Polyelectrolyte multilayers (PEMs) were assembled by means of alternate electrostatic adsorption of polyanions and polycations using colloidal structure of polyelectrolyte complexes (PECs) as LbL building blocks. High enzyme concentrations were introduced into polyethyleneimine (PEI), a positively charged polyelectrolyte solution, to form an electrostatic PECs with dextran sulfate (DS), a negatively charged polye
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Busono, Pratondo. "Development of Amperometric Biosensor Immobilized by Entrapment of Urease Enzyme in Polypiroll Film for the Determination of Blood Urea." In 2014 International Conference on Physics and its Applications. Atlantis Press, 2015. http://dx.doi.org/10.2991/icopia-14.2015.23.

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