An Aminotransferase from Enhydrobacter aerosaccus to Obtain Optically Pure β-Phenylalanine.

ABSTRACT: An aminotransferase ω-TAEn was identified from Enhydrobacter aerosaccus. The ω-TAEn was successfully expressed in Escherichia coli and the obtained enzyme showed activity toward β-phenylalanine (β-phe) at optimal conditions. For optically pure (R)-β-phe, 50% yield was observed by kinetic resolution of racemic amino with pyruvate as the amino acceptor. To obtain (S)-β-phe, the lipase/ω-TAEn catalytic system was adopted. The ω-TAEn showed strict stereoselectivity to the amino donor. The formation of (S)-β-phe was observed using 3-aminobutyric acid as the amino donor, and (S)-β-phe was obtained by asymmetric synthesis with a yield of 82%.

SUBMITTER: Feng X 

PROVIDER: S-EPMC7160847 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature