Kinetic Resolution of α-methylbenzylamine by Recombinant Pichia pastoris Expressing ω-transaminase

Recombinant Pichia pastoris expressing ω-transaminase (TA) was used as a whole-cell biocatalyst to kinetically resolve α-methylbenzylamine (MBA). To overcome product inhibition of ω-TA by acetophenone (deaminated product of α-MBA), the reaction condition of endogenous oxidoreductases, which can cata...

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Published in:Biotechnology and bioprocess engineering 2010, 15(3), , pp.429-434
Main Authors: Bea, H.S., Yeungnam University, Gyeongsan, Republic of Korea, Seo, Y.M., Yeungnam University, Gyeongsan, Republic of Korea, Cha, M.H., Seoul National University, Seoul, Republic of Korea, Kim, B.G., Seoul National University, Seoul, Republic of Korea, Yun, H.D., Yeungnam University, Gyeongsan, Republic of Korea
Format: Article
Language:English
Subjects:
Biotechnology
Chemistry
Chemistry and Materials Science
chiral amines
Industrial and Production Engineering
kinetic resolution
omega-transaminase
PICHIA PASTORIS
recombinant Pichia pastoris
Research Paper
생물공학
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Summary:Recombinant Pichia pastoris expressing ω-transaminase (TA) was used as a whole-cell biocatalyst to kinetically resolve α-methylbenzylamine (MBA). To overcome product inhibition of ω-TA by acetophenone (deaminated product of α-MBA), the reaction condition of endogenous oxidoreductases, which can catalyze the reduction of acetophenone into non-inhibitory 1-phenylethanol, was optimized. When the whole-cell reaction was carried out using recombintat P. pastoris in 100 mM Tris/HCl buffer (pH 9.0) containing 2.5% glucose and 1% methanol, 100 mM α-MBA was successfully resolved to (R)-α-MBA (greater than 99% ee) at a conversion of 52.2%.
ISSN:1226-8372
1976-3816
DOI:10.1007/s12257-009-3093-1