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Catalysts 2017, 7(4), 112; doi:10.3390/catal7040112

Improving the Stability of Cold-Adapted Enzymes by Immobilization

1
Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan 38453, Korea
2
Department of Biological Sciences and Biotechnology, Hannam University, Daejeon 34054, Korea
*
Author to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Received: 13 January 2017 / Revised: 30 March 2017 / Accepted: 4 April 2017 / Published: 12 April 2017
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
View Full-Text   |   Download PDF [629 KB, uploaded 19 April 2017]   |  

Abstract

Cold-adapted enzymes have gained considerable attention as biocatalysts that show high catalytic activity at low temperatures. However, the use of cold-adapted enzymes at ambient temperatures has been hindered by their low thermal stabilities caused by their inherent structural flexibilities. Accordingly, protein engineering and immobilization have been employed to improve the thermal stability of cold-adapted enzymes. Immobilization has been shown to increase the thermal stability of cold-adapted enzymes at the critical temperatures at which denaturation begins. This review summarizes progress in immobilization of cold-adapted enzymes as a strategy to improve their thermal and organic solvent stabilities. View Full-Text
Keywords: cold-adapted enzymes; immobilization; thermal stability; organic solvent stability cold-adapted enzymes; immobilization; thermal stability; organic solvent stability
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Lee, C.; Jang, S.-H.; Chung, H.-S. Improving the Stability of Cold-Adapted Enzymes by Immobilization. Catalysts 2017, 7, 112.

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