Reductive enzymatic dynamic kinetic resolution affording 115 g/L (S)-2-phenylpropanol.

ABSTRACT:

Background

Published biocatalytic routes for accessing enantiopure 2-phenylpropanol using oxidoreductases afforded maximal product titers of only 80 mM. Enzyme deactivation was identified as the major limitation and was attributed to adduct formation of the aldehyde substrate with amino acid residues of the reductase.

Results

A single point mutant of Candida tenuis xylose reductase (CtXR D51A) with very high catalytic efficiency (43·10³ s^-1 M^-1) for (S)-2-phenylpropanal was found. The enzyme showed high enantioselectivity for the (S)-enantiomer but was deactivated by 0.5 mM substrate within 2 h. A whole-cell biocatalyst expressing the engineered reductase and a yeast formate dehydrogenase for NADH-recycling provided substantial stabilization

SUBMITTER: Rapp C 

PROVIDER: S-EPMC8507385 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature