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Immobilized enzyme

About: Immobilized enzyme is a research topic. Over the lifetime, 15282 publications have been published within this topic receiving 401860 citations.


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Journal ArticleDOI
TL;DR: It is demonstrated that just 2.5 kg of immobilized enzyme may be sufficient to degrade 30,000 tons of nerve agent in just 1 year.
Abstract: Phosphotriesterase (EC 3.1.8.1) was immobilized within a polyurethane foam matrix during polymer synthesis using a prepolymer synthesis strategy. In addition to retaining greater than 50% of the enzyme specific activity, numerous benefits were incurred upon immobilization. Orders of magnitude increases in storage and thermal stability (net stabilization energy = 12.5 kJ/mol) were observed without the need for enzyme premodification. The immobilized enzyme system was protease resistant and seemed to display no adverse effects from immobilization, such as an alteration of enzyme function. The organic solvent, dimethyl sulfoxide, also exhibited a stabilizing effect on phosphotriesterase enzyme systems over a range of intermediate concentrations. We attribute these effects in part to direct interaction between the aprotic solvent and metal containing residues present at the enzyme's active site. Our data demonstrate that just 2.5 kg of immobilized enzyme may be sufficient to degrade 30,000 tons of nerve agent in just 1 year. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 54: 105–114, 1997.

113 citations

Journal ArticleDOI
TL;DR: In this article, the methyl esters of the long chain fatty acids (biodiesel) were synthesized by methanolysis of canola oil by immobilized lipase Lipase from Thermomyces lanuginosus was immobilized by both physical adsorption and covalent attachment onto polyglutaraldehyde activated styrene-divinylbenzene (STY-DVB) copolymer.

113 citations

Journal ArticleDOI
TL;DR: The complex enzyme preparation containing both exo- and endoinulinases was immobilized covalently onto a porous cellulose derivative, Amino-Cellulofine, by the carbodiimide method at pH 5.0, and the immobilized enzyme was stable in the pH ranges of 4.5 to 6.0 and up to 60°C.

113 citations

Journal ArticleDOI
TL;DR: The immobilized enzyme was found to be stabilized compared to the free enzyme, and the performance of the biocatalyst was evaluated by the degradation of phenolic compounds including phenol, p-chlorophenol and catechol.

113 citations

Journal ArticleDOI
TL;DR: The preparations and performances of the novel amperometric biosensors for glucose based on immobilized glucose oxidase (GOD) on modified Pt electrodes are described and the effect of applied potential, thickness of the polymeric film, amount of the immobilized enzyme, pH, the amounts of the deposited Au, temperature and substrate concentration on the responses of the biosensor were investigated.

113 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023219
2022417
2021480
2020548
2019553
2018543