Topic
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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TL;DR: An overview of the behavior of enzymes immobilized on nanomaterials is examined and the results reported with such biocatalyst preparations are discussed.
Abstract: Nanomaterials constitute novel and interesting matrices for enzyme immobilization. While their high surface to volume ratio is an obvious advantage, their Brownian motion can impact the behavior of enzymes immobilized on these matrices. Carbon nanotubes, superparamagnetic nanoparticles, and mesoporous materials constitute some important classes of matrices. Such immobilized enzyme systems have been used in both aqueous and low water media for biocatalysis and resolution of racemates. This overview examines the behavior of enzymes immobilized on nanomaterials and discusses the results reported with such biocatalyst preparations.
134 citations
TL;DR: This review summarizes selected studies that have used immobilization to tailor the catalytic properties of enzymes, and highlights the application of immobilizing to the rational design of biocatalysts.
133 citations
TL;DR: This experimental work represents a first attempt at construction of a new carbon nanotube-tyrosinase based biosensor able to determine the concentration of BPA, one of the most ubiquitous and hazardous endocrine disruptors which can pollute the drinking and surface water, as well as many products of the food chain.
133 citations
TL;DR: This article highlights the different strategies for enzyme immobilization such as physical adsorption, covalent binding, co-ordination bonding and de novo encapsulation method and about the artificial enzyme properties of magnetic-MOF coupled with enzyme to extend its application in biosensor.
133 citations
TL;DR: Numerical simulations were developed that incorporate spatially heterogeneous catalytic and inactivation processes that are consistent with the reaction of hydrogen peroxide and certain catalytic intermediates of both enzymes.
Abstract: Homogeneous membranes containing immobilized glucose oxidase and catalase were stored in buffered solutions at 37 degrees C to determine the mechanisms and rates of catalyst inactivation. The experiments were designed so that inactivation occurred homogeneously throughout the membrane, thereby simplifying the analysis. The mechanism of inactivation is consistent with the reaction of hydrogen peroxide and certain catalytic intermediates of both enzymes. Based on this information, numerical simulations were developed that incorporate spatially heterogeneous catalytic and inactivation processes.
133 citations