Efficient kinetic resolution of para-chlorostyrene oxide at elevated concentration by Solanum lycopersicum epoxide hydrolase in the presence of Tween-20

• Published in: Catalysis communications 2021-01, Vol.149, p.106180, Article 106180
• Main Authors: Wen, Zheng, Hu, Bo-Chun, Hu, Die, Liu, You-Yi, Zhang, Dong, Zang, Jia, Wu, Min-Chen
• Format: Article
• Language: English
• Subjects: Enantioselective hydrolysis; Epoxide hydrolase; para-Chlorostyrene oxide; Solanum lycopersicum; Tween-20
• ISSN: 1566-7367; 1873-3905
• DOI: 10.1016/j.catcom.2020.106180

A putative Solanum lycopersicum epoxide hydrolase, SlEH2, was discovered based on computer-aided analysis. Then, its encoding gene (sleh2) was expressed in E. coli BL21(DE3). The substrate spectrum assay exhibited that E. coli/sleh2, an E. coli transformant expressing SlEH2, possessed the activity of 74.8 U/g wet cell and enantiomeric ratio (E) of 145 towards racemic (rac-) para-chlorostyrene oxide (4a). The scale-up kinetic resolution of 400 mM rac-4a was conducted using 200 mg/mL wet cells of E. coli/sleh2 in the presence of 1% (v/v) Tween-20, retaining (R)-4a with 98.4% ees and 47.1% yields while affording (R)-4b with 92.0% eep and 49.5% yieldp. [Display omitted] •An S. lycopersicum epoxide hydrolase, SlEH2, was discovered via computer-aided analysis.•E. coli/sleh2 had an EH activity of 74.8 U/g wet cell and a large E of 145 towards rac-4a.•The αS and βR of purified SlEH2 for (S)- and (R)-4a were 98.7 and 58.5%, respectively.•Hydrolysis of 400 mM rac-4a was efficiently conducted in the presence of 1% (v/v) Tween-20.