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Journal of Food Science and Biotechnology

Corresponding Author(s)

孙付保(1975—),男,博士,教授,博士研究生导师,主要从事高活性蛋白肽、氨基酸的绿色生物制造技术研究。E-mail:fubaosun@jiangnan.edu.cn

Abstract

[Objective ] This study aims to establish the biosynthesis process of N-acetyl- trans -4-hydroxyproline (N-ATHOP ).[Method ] Escherichia coli (E.coli ) BL21 (DE3) was selected as the host to heterologously express the acyltransferase (MsAcT ) derived from Mycobacterium smegmatis.A semi-rational design was employed to construct the mutant MsAcT (S11C) capable of catalyzing the synthesis of N-ATHOP.[Result ] The catalytic reaction conditions of the mutant MsAcT (S11C) were optimized as pH 6.9,reaction temperature 49 ℃,initial trans -4-hydroxyproline (THOP ) concentration of 315.5 mmol/L,and vinyl acetate volume fraction of 10%.Under the optimized conditions,the yield of N-ATHOP synthesized under the catalysis of MsAcT (S11C) reached 4.71 g/L,with a conversion rate of 10.95% after 12 h of reaction.[Conclusion ] The mutant MsAcT (S11C) successfully achieved microbial enzymatic biosynthesis from THOP to N-ATHOP.

Publication Date

7-15-2025

First Page

85

Last Page

93

DOI

10.12441/spyswjs.20240320002

References

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