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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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Journal ArticleDOI

Covalent attachment of trypsin on plasma polymerized allylamine.

TL;DR: UV-vis absorption spectroscopy showed that allylamine plasma polymer presents a high adsorption yield of trypsin, and the highest catalytic activity obtained was for the enzymes that underwent the three steps of the immobilization process.
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Medium optimization and immobilization of purified fibrinolytic URAK from Bacillus cereus NK1 on PHB nanoparticles

TL;DR: In this paper, an organism primarily isolated from soil, identified as Bacillus cereus NK1 was found to secrete an extracellular protease and the enzyme was identified to degrade fibrin.
Journal ArticleDOI

Highly enantioselective biocatalysts by coating immobilized lipases with polyethyleneimine

TL;DR: Polyethyleneimine modification on immobilized lipases greatly enhanced their enantioselectivity in the kinetic resolution of (±)-2-hydroxy-phenylacetic acid methyl ester and improved the stability of the biocatalyst at high temperatures and in the presence of high co-solvent concentrations.
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Superior activities of lipase immobilized on pure and hydrophobic clay supports: Characterization and catalytic activity studies

TL;DR: Immobilized lipases exhibited enhanced storage stability than the native lipase (up to 40 days) and the free lipase was 195-fold more active in water compared to that in organic solvent.
Journal ArticleDOI

Enzyme activity assay for horseradish peroxidase encapsulated in peptide nanotubes.

TL;DR: It is proved that the encapsulation of HRP inside the PNT may be an effective way to keep the enzyme activity stable in various environments.
References
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Journal ArticleDOI

Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking.

TL;DR: An overview of glutaraldehyde as a crosslinking reagent is given by describing its structure and chemical properties in aqueous solution in an attempt to explain its high reactivity toward proteins, particularly as applied to the production of insoluble enzymes.
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A serine protease triad forms the catalytic centre of a triacylglycerol lipase.

TL;DR: The X-ray structure of the Mucor miehei triglyceride lipase is reported and the atomic model obtained reveals a Ser .. His .. Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.
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A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex

TL;DR: It is proposed that the structure of the enzyme in this complex of R. miehei lipase with n-hexylphosphonate ethyl ester is equivalent to the activated state generated by the oil–water interface.
Book

Enzymes in synthetic organic chemistry

TL;DR: Part 1 general aspects: rate acceleration in enzyme-catalyzed reactions Michaelis-Menten kinetics enzyme inhibition specificity improvement or alteration of enzyme specifity enzyme stabilization and reactor configuration cofactor regeneration enzyme catalysis in organic solvents multienzyme systems and metabolic engineering rational design of new enzymatic catalysts references.
Journal ArticleDOI

Enzymes for chemical synthesis

TL;DR: Enzyme-catalysed chemical transformations are now widely recognized as practical alternatives to traditional (non-biological) organic synthesis, and as convenient solutions to certain intractable synthetic problems.
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