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KMID : 1094720100150030429
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Biotechnology and Bioprocess Engineering
2010 Volume.15 No. 3 p.429 ~ p.434
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Kinetic Resolution of α-methylbenzylamine by Recombinant Pichia pastoris Expressing ω-transaminase
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Bea Han-Seop
Seo Young-Man
Cha Min-Ho
Kim Byung-Gee
Yun Hyung-Don
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Abstract
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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 (> 99% ee) at a conversion of 52.2%.
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KEYWORD
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kinetic resolution, recombinant Pichia pastoris, chiral amines, ω-transaminase
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