Improving Theaflavin-3,3'-digallate Production Efficiency Optimization by Transition State Conformation of Polyphenol Oxidase.

ABSTRACT: Theaflavins (TFs) are good for health because of their bioactivities. Enzymatic synthesis of TFs has garnered much attention; however, the source and activity of the enzymes needed limit their wide application. In this study, a microbial polyphenol oxidase from Bacillus megaterium was screened for the synthesis of theaflavin-3,3'-digallate (TFDG). Based on structural and mechanistic analyses of the enzyme, the O-O bond dissociation was identified as the rate-determining step. To address this issue, a transition state (TS) conformation optimization strategy was adopted to stabilize the spatial conformation of the O-O bond dissociation, which improved the catalytic efficiency of tyrosinase. Under the optimum transformation conditions of pH 4.0, temperature 25 °C, (-)-epigallocatechin

SUBMITTER: Huang Y 

PROVIDER: S-EPMC10179947 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature