详细信息
Production of enantiomerically pure (S)-β-phenylalanine and (R)-β-phenylalanine by penicillin G acylase from Escherichia coli in aqueous medium ( SCI-EXPANDED收录)
文献类型:期刊文献
英文题名:Production of enantiomerically pure (S)-β-phenylalanine and (R)-β-phenylalanine by penicillin G acylase from Escherichia coli in aqueous medium
作者:Li, Dengchao; Cheng, Shiwei; Wei, Dongzhi; Ren, Yuhong; Zhang, Derong
机构:[1]E China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China
年份:2007
卷号:29
期号:12
起止页码:1825
外文期刊名:BIOTECHNOLOGY LETTERS
收录:;WOS:【SCI-EXPANDED(收录号:WOS:000250537700005),CCR-EXPANDED(收录号:WOS:000250537700005)】;
语种:英文
外文关键词:acylation; enantiomeric excess; penicillin G acylase; phenylacetamide; beta-Phenylalanine
摘要:A new approach has been developed for the production of enantiomerically pure (S)-beta-phenylalanine (S-BPA) and (R)-beta-phenylalanine in aqueous medium based on enantioselective acylation and hydrolysis properties of penicillin G acylase from Escherichia coli. The acylation reaction was highly preferential for the acylation of (R)-BPA to form N-phenylacetyl-(R)-BPA using phenylacetamide as an acyl donor, which was separated and then hydrolyzed to (R)-BPA by the same enzyme at pH 7.5. The optimal acylation reaction was at pH 10, 25 degrees C with a 2:1 molar ratio of phenylacetamide to BPA, 8 IU ml(-1) enzyme and 150 mM BPA. These resulted in a conversion of about 50% BPA; enantiomeric excess of (S)-BPA and (R)-BPA separated were 98 and 99%, respectively.
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