Pan_2024_Enzyme.Microb.Technol_183_110547

Reference

Title : Screening of lipase TiL from Tilletia indica for chemo-enzymatic epoxidation of alkenes - Pan_2024_Enzyme.Microb.Technol_183_110547
Author(s) : Pan J , Yang N , Lv YL , Zhang ZY , Li CX , Xu JH
Ref : Enzyme Microb Technol , 183 :110547 , 2024
Abstract :

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.

PubMedSearch : Pan_2024_Enzyme.Microb.Technol_183_110547
PubMedID: 39591727
Gene_locus related to this paper: 9basi-a0a177tt48

Related information

Substrate Methyl-octanoate
Gene_locus 9basi-a0a177tt48

Citations formats

Pan J, Yang N, Lv YL, Zhang ZY, Li CX, Xu JH (2024)
Screening of lipase TiL from Tilletia indica for chemo-enzymatic epoxidation of alkenes
Enzyme Microb Technol 183 :110547

Pan J, Yang N, Lv YL, Zhang ZY, Li CX, Xu JH (2024)
Enzyme Microb Technol 183 :110547