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Recent advances in the improvement of enzyme thermostability by structure modification.

Authors
  • Xu, Zhe1, 2
  • Cen, Yu-Ke1, 2
  • Zou, Shu-Ping1, 2
  • Xue, Ya-Ping1, 2
  • Zheng, Yu-Guo1, 2
  • 1 Key Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China. , (China)
  • 2 Engineering Research Center of Bioconversion and Biopurification of Ministry of Education, Zhejiang University of Technology, Hangzhou, China. , (China)
Type
Published Article
Journal
Critical reviews in biotechnology
Publication Date
Feb 01, 2020
Volume
40
Issue
1
Pages
83–98
Identifiers
DOI: 10.1080/07388551.2019.1682963
PMID: 31690132
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Thermostability is considered to be an important parameter to measure the feasibility of enzymes for industrial applications. Generally, higher thermostability makes an enzyme more competitive and desirable in industry. However, most natural enzymes show poor thermostability, which restricts their application. Protein structure modification is a desirable method to improve enzyme properties. In recent years, tremendous progress has been achieved in protein thermostability engineering. In this review, we provide a systemic overview on the approaches of protein structure modification for the improvement of enzyme thermostability during the last decade. Structure modification approaches, including the introduction of non-covalent interactions and covalent bonds, increase of proline and/or decrease in glycine, reinforcement of subunit-subunit interactions, introduction of glycosylation sites, truncation and cyclization have been highlighted.

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