Kinetic Resolution of alpha-methylbenzylamine by Recombinant Pichia pastoris Expressing omega-transaminase

Title
Kinetic Resolution of alpha-methylbenzylamine by Recombinant Pichia pastoris Expressing omega-transaminase
Author(s)
윤형돈배한섭[배한섭]서영만[서영만]차민호[차민호]김병기[김병기]
Keywords
ASYMMETRIC-SYNTHESIS; CHIRAL AMINES; CLONING
Issue Date
201006
Publisher
KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
Citation
BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.15, no.3, pp.429 - 434
Abstract
Recombinant Pichia pastoris expressing omega-transaminase (TA) was used as a whole-cell biocatalyst to kinetically resolve alpha-methylbenzylamine (MBA). To overcome product inhibition of omega-TA by acetophenone (deaminated product of alpha-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 alpha-MBA was successfully resolved to (R)-alpha-MBA (> 99% ee) at a conversion of 52.2%.
URI
http://hdl.handle.net/YU.REPOSITORY/22332http://dx.doi.org/10.1007/s12257-009-3093-1
ISSN
1226-8372
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생명공학부 > 생명공학부 > Articles
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