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Improvement of enzyme activity, stability and selectivity via immobilization techniques

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TLDR
In all cases, enzyme engineering via immobilization techniques is perfectly compatible with other chemical or biological approaches to improve enzyme functions and the final success depend on the availability of a wide battery of immobilization protocols.
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This article is published in Enzyme and Microbial Technology.The article was published on 2007-05-02. It has received 3016 citations till now. The article focuses on the topics: Immobilized enzyme.

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Citations
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Journal ArticleDOI

Modifying enzyme activity and selectivity by immobilization.

TL;DR: In this tutorial review, some of the main reasons that may produce an improvement in enzyme activity, specificity or selectivity, either real or apparent, due to immobilization are listed.
Journal ArticleDOI

Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance

TL;DR: The advantages and disadvantages of the different existing immobilization strategies to solve the different aforementioned enzyme limitations are given and some advice to select the optimal strategy for each particular enzyme and process is given.
Journal ArticleDOI

Understanding enzyme immobilisation

TL;DR: This tutorial review focuses on the understanding of enzyme immobilisation, which can address the issue of enzymatic instability.
Journal ArticleDOI

Enzyme stability and stabilization—Aqueous and non-aqueous environment

TL;DR: An overview of the denaturation mechanisms in aqueous and non-aqueous environment is given in this article, and various methods of enzyme stabilization with respect to their use in the aqueously and nonaqueous environments have been given.
Journal ArticleDOI

Polymer biodegradation: mechanisms and estimation techniques.

TL;DR: The aim of this review is to emphasise the importance of measure as well as possible, the last stage of the biodegradation, in order to certify the integration of new materials into the biogeochemical cycles.
References
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Journal ArticleDOI

Preparation of a very stable immobilized biocatalyst of glucose oxidase from Aspergillus niger.

TL;DR: The adsorption of GOX on aminated cationic support and subsequent treatment with glutaraldehyde was presented as a very successful methodology for achieving a very stable biocatalyst.
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Characterization of Thermoanaerobacter cyclomaltodextrin glucanotransferase immobilized on glyoxyl-agarose

TL;DR: The immobilization of the Thermoanaerobacter cyclomaltodextrin glucanotransferase (CGTase) enzyme into cross-linked 6% agarose beads activated by high density of linear aldehyde groups (glyoxyl-agarose) that allow the establishment of multi-attachment enzyme-support bonds are presented.
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Stabilization of heterodimeric enzyme by multipoint covalent immobilization: Penicillin G acylase from Kluyvera citrophila.

TL;DR: In this article, the authors developed a strategy for immobilization-stabilization of penicillin G acylase (PGA) from Kluyvera citrophila by controlled multipoint covalent attachment to agarose-aldehyde gels.
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Biotransformations catalyzed by multimeric enzymes: stabilization of tetrameric ampicillin acylase permits the optimization of ampicillin synthesis under dissociation conditions.

TL;DR: Synthetic yields improved from around 65%, under conditions where the nonstabilized derivative was stable, to around 85% in conditions where only the stabilized derivative could be utilized, and when using high concentrations of PGM, a significant worsening of the reaction performance was detected with a significant decrease in the yields.
Journal Article

Dissociative thermal inactivation, stability, and activity of oligomeric enzymes

TL;DR: The relations which allow the calculation from experimental data the following physicochemical constants which characterize the stability of oligomeric enzymes are given: the constant for the rate of irreversible change of monomeric protein, the equilibrium constant for dimer dissociation, and the rate constant for dissociation.
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