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酶的寡聚结构与催化稳定性

刘护 李春

化工学报2018,Vol.69Issue(1):352-362,11.
化工学报2018,Vol.69Issue(1):352-362,11.DOI:10.11949/j.issn.0438-1157.20171058

酶的寡聚结构与催化稳定性

Oligomeric structure of enzyme and its catalysis stability

刘护 1李春1

作者信息

  • 1. 北京理工大学化学与化工学院生化工程系,北京 100081
  • 折叠

摘要

Abstract

The structure and catalytic stability of enzymes are of intriguing interest in biocatalysis and biotransformation.Compared with monomeric enzymes, the subunit self-assembling of oligomeric enzymes brings superior structural and functional properties.However, a series of problems also exist in the course of preparation and application of oligomeric enzymes, such as poor preparation efficiency, lower utilization of catalytic sites and less catalytic stability.Among them, the weak catalytic stability resulting from subunits dissociation severely limits the wider industrial applications of oligomeric enzymes.Currently, medium engineering, multi-subunit immobilization, subunit interface engineering and fusion protein strategy have been used to improve the oligomeric enzyme stability.Besides, the design strategy of transforming oligomeric enzymes into monomers attempts to solve the preparation and application problems fundamentally and has an extensive application prospect.In this paper, the desirable functions generated by oligomeric enzyme evolution were introduced first.Then, the preparation and application problems were summarized.At last, the strategies for improving oligomeric enzyme preparation and stabilization were reviewed.

关键词

生物催化//稳定性/寡聚酶/单体酶/结构演替

Key words

biocatalysis/enzyme/stability/oligomeric enzyme/monomeric enzyme/structural succession

分类

生物科学

引用本文复制引用

刘护,李春..酶的寡聚结构与催化稳定性[J].化工学报,2018,69(1):352-362,11.

基金项目

国家自然科学基金项目(21706012,21425624) (21706012,21425624)

中国博士后科学基金面上资助(2016M600936). supported by the National Natural Science Foundation of China (21706012,21425624) and the China Postdoctoral Science Foundation Funded Project(2016M600936). (2016M600936)

化工学报

OA北大核心CSCDCSTPCD

0438-1157

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