Rational Design for Enhanced Acyltransferase Activity in Water Catalyzed by the Pyrobaculum calidifontis VA1 Esterase.

ABSTRACT: Biocatalytic transesterification is commonly carried out employing lipases in anhydrous organic solvents since hydrolases usually prefer hydrolysis over acyl transfer in bulk water. However, some promiscuous acyltransferases can catalyze acylation in an aqueous solution. In this study, a rational design was performed to enhance the acyltransferase selectivity and substrate scope of the Pyrobaculum calidifontis VA1 esterase (PestE). PestE wild type and variants were applied for the acylation of monoterpene alcohols. The mutant PestE_I208A is selective for (-)-menthyl acetate (E-Value = 55). Highly active acyltransferases were designed, allowing for complete conversion of (-)-citronellol to citronellyl acetate. Additionally, carvacrol was acetylated but with lower conversions. To the

SUBMITTER: Staudt A 

PROVIDER: S-EPMC8402108 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature