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 ( EI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[1]; Cheng, Shiwei[1]; Wei, Dongzhi[1]; Ren, Yuhong[1]; Zhang, Derong[1]
机构:[1] State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, China
年份:2007
卷号:29
期号:12
起止页码:1825
外文期刊名:Biotechnology Letters
收录:EI(收录号:20074510910918)
语种:英文
外文关键词:Acylation - Enantioselectivity - Enzymes - Escherichia coli - Hydrolysis
摘要:A new approach has been developed for the production of enantiomerically pure (S)-β-phenylalanine (S-BPA) and (R)-β-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°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. ? 2007 Springer Science+Business Media B.V.
参考文献:
正在载入数据...
