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


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

SUBMITTER: Feng X 

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

REPOSITORIES: biostudies-literature

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An Aminotransferase from <i>Enhydrobacter aerosaccus</i> to Obtain Optically Pure β-Phenylalanine.

Feng Xinming X   Guo Jing J   Zhang Rubing R   Liu Wei W   Cao Yujin Y   Xian Mo M   Liu Huizhou H  

ACS omega 20200402 14


An aminotransferase ω-TAEn was identified from <i>Enhydrobacter aerosaccus</i>. The ω-TAEn was successfully expressed in <i>Escherichia coli</i> and the obtained enzyme showed activity toward β-phenylalanine (β-phe) at optimal conditions. For optically pure (<i>R</i>)-β-phe, 50% yield was observed by kinetic resolution of racemic amino with pyruvate as the amino acceptor. To obtain (<i>S</i>)-β-phe, the lipase/ω-TAEn catalytic system was adopted. The ω-TAEn showed strict stereoselectivity to the  ...[more]

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