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

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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%.

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Feng, X., Guo, J., Zhang, R., Liu, W., Cao, Y., Xian, M., & Liu, H. (2020). An Aminotransferase from Enhydrobacter aerosaccus to Obtain Optically Pure β-Phenylalanine. ACS Omega, 5(14), 7745–7750. https://doi.org/10.1021/acsomega.9b03416

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