Next Article in Journal
Abatement of VOCs Using Packed Bed Non-Thermal Plasma Reactors: A Review
Previous Article in Journal
Unprecedented Multifunctionality of Grubbs and Hoveyda–Grubbs Catalysts: Competitive Isomerization, Hydrogenation, Silylation and Metathesis Occurring in Solution and on Solid Phase
Previous Article in Special Issue
Stabilization of a Lipolytic Enzyme for Commercial Application
Open AccessReview

Improving the Stability of Cold-Adapted Enzymes by Immobilization

Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan 38453, Korea
Department of Biological Sciences and Biotechnology, Hannam University, Daejeon 34054, Korea
Author to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Catalysts 2017, 7(4), 112;
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)
PDF [629 KB, uploaded 19 April 2017]


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

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Lee, C.; Jang, S.-H.; Chung, H.-S. Improving the Stability of Cold-Adapted Enzymes by Immobilization. Catalysts 2017, 7, 112.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Catalysts EISSN 2073-4344 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top