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Enantioselective hydrolysis of hydrophobic amino acid derivatives by lipases
Authors:Aih-Jing Chiou  Shih-Hsiung Wu  Kung-Tsung Wang
Affiliation:(1) Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, ROC;(2) Graduate Institute of Biochemical Sciences, National Taiwan University, P. O. Box. 23-106, Taipei, Taiwan, ROC
Abstract:Microbial lipases preferentially cleave the L-isomers of N-benzyloxycarbonyl (Z)-hydrophobic D,L-amino acid methyl esters which is the same as that of subtilisin. This implies that lipases and proteases may share the same ancestor in the evolutionary point and lipases can be practically applied to resolve racemic hydrophobic amino acid derivatives.
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