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Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization

Paper ID Volume ID Publish Year Pages File Format Full-Text
17280 42657 2011 21 PDF Available
Title
Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization
Abstract

The immobilization of proteins (mostly typically enzymes) onto solid supports is mature technology and has been used successfully to enhance biocatalytic processes in a wide range of industrial applications. However, continued developments in immobilization technology have led to more sophisticated and specialized applications of the process. A combination of targeted chemistries, for both the support and the protein, sometimes in combination with additional chemical and/or genetic engineering, has led to the development of methods for the modification of protein functional properties, for enhancing protein stability and for the recovery of specific proteins from complex mixtures. In particular, the development of effective methods for immobilizing large multi-subunit proteins with multiple covalent linkages (multi-point immobilization) has been effective in stabilizing proteins where subunit dissociation is the initial step in enzyme inactivation. In some instances, multiple benefits are achievable in a single process.Here we comprehensively review the literature pertaining to immobilization and chemical modification of different enzyme classes from thermophiles, with emphasis on the chemistries involved and their implications for modification of the enzyme functional properties. We also highlight the potential for synergies in the combined use of immobilization and other chemical modifications.

Keywords
Thermophilic enzymes; Enzyme immobilization; Enzyme stabilization; Chemical modification of enzymes; Modulation of enzyme properties
First Page Preview
Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 49, Issue 4, 10 September 2011, Pages 326–346
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering