LIU Hu, LI Chun. Oligomeric structure of enzyme and its catalysis stability[J]. CIESC Journal, 2018, (1): 352-362.DOI: 10.11949/j.issn.0438-1157.20171058.
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.