Oligomeric structure of enzyme and its catalysis stability

Hu Liu, Chun Li*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)352-362
Number of pages11
JournalHuagong Xuebao/CIESC Journal
Volume69
Issue number1
DOIs
Publication statusPublished - 1 Jan 2018

Keywords

  • Biocatalysis
  • Enzyme
  • Monomeric enzyme
  • Oligomeric enzyme
  • Stability
  • Structural succession

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