4.5 Review

Enzyme stabilization -: recent experimental progress

Journal

ENZYME AND MICROBIAL TECHNOLOGY
Volume 33, Issue 2-3, Pages 137-149

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/S0141-0229(03)00160-1

Keywords

enzyme stabilization; inactivation model; protein engineering; directed evolution; chemical modification; stabilizing additives

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This article surveys the enzyme stabilization literature since 1997, focusing on protein engineering and chemical modification. Within protein engineering, directed evolution strategies have yielded notable successes. Polypeptide chain extension, manipulation of chimeric proteins and rational design have also led to stability gains. Chemical modification, as manifested in crosslinked enzyme crystals (CLECs), covalent attachment of polymers and surface modification, remains useful. Inactivation models, stabilizing additives and organic solvents also receive mention. Since extremophilic proteins have received much attention elsewhere, recent reviews are merely indicated. Immobilized proteins are not considered; neither is the computational design or prediction of protein stability. Case studies focus on enzymes used, or potentially useful, in industrial processes or in biosensors. Examples include peroxidases, phospholipase, cellulase, phytase, luciferase, bacterial proteases, alpha-amylase and glucose isomerase (GI), among others. (C) 2003 Elsevier Inc. All rights reserved.

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