Screening of lipase TiL from Tilletia indica for chemo-enzymatic epoxidation of alkenes

被引：0

作者：

Pan, Jiang ^{[1
]}

Yang, Nan ^{[1
]}

Lv, Yuan-Lin ^{[1
]}

Zhang, Zi-Yang ^{[1
]}

Li, Chun-Xiu ^{[1
]}

Xu, Jian-He ^{[1
]}

机构：

[1] East China Univ Sci & Technol, Lab Biocatalysis & Synthet Biotechnol, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 2025年 / 183卷

关键词：

Chemo-enzymatic epoxidation; Tilletia indica Lipase; Methyl oleate; alpha-Pinene; MEDIATED EPOXIDATION; PEROXYCARBOXYLIC ACIDS; METHYL OLEATE; CATALYZED SYNTHESIS; ALPHA-PINENE;

D O I：

10.1016/j.enzmictec.2024.110547

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Lipase can mediate the chemo-enzymatic epoxidation of alkenes with the presence of free carboxylic acid and hydrogen peroxide. Four novel lipases with the abilities of chemo-enzymatic epoxidation were mined from the gene database. Lipase TiL originated from Tilletia indica was identified with significant activity on formation of methyl epoxystearate from methyl oleate. n-Heptanoic acid was determined as the optimal carboxylic acid substrate of TiL. Methyl oleate and alpha-pinene were efficiently converted to corresponding epoxy compound in micro-aqueous media and aqueous-organic biphase, respectively. A preparative scale chemo-enzymatic transformation of alpha-pinene was conduct using the optimized reaction condition, with 30 % yield of alpha-pinene oxide obtained.

引用

页数：7

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