文献类型：期刊文献

英文题名：Efficient asymmetric synthesis of D-N-formyl-phenylglycine via cross-linked nitrilase aggregates catalyzed dynamic kinetic resolution

作者：Qiu, Jian[1];Su, Erzheng[1,2];Wang, Wei[1];Wei, Dongzhi[1]

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, New World Inst Biotechnol, Shanghai 200237, Peoples R China;[2]Nanjing Forestry Univ, Coll Light Ind Sci & Engn, Enzyme & Fermentat Technol Lab, Nanjing 210037, Jiangsu, Peoples R China

年份：2014

卷号：51

起止页码：19

外文期刊名：CATALYSIS COMMUNICATIONS

收录：;EI(收录号：20141617573882);WOS:【SCI-EXPANDED(收录号:WOS:000336469200005)】；

基金：This work was supported by the National Basic Research Program of China (No. 2012CB721003) and the Fundamental Research Funds for the Central Universities (WF1013008).

语种：英文

外文关键词：Nitrilase; Cross-linked enzyme aggregates; Dynamic kinetic resolution; D-N-formyl-phenylglycine

摘要：In this study, a nitrilase-CLEA mediated dynamic kinetic resolution for the asymmetric synthesis of D-N-formylphenylglycine was developed. Cross-linked enzyme aggregates (CLEAs) of nitrilase from Sphingomonas wittichii RW1 were first prepared and characterized. Compared with the free nitrilase, nitrilase-CLEAs showed higher stability against various conditions such as pH and temperature. The nitrilase-CLEA catalyzed dynamic kinetic resolution of N-formyl-phenylglycinonitrile was further optimized. Under the optimal conditions, the yield and ee value of N-D-formyl-phenylglycine achieved 95% and 97%, respectively. Additionally, the nitrilase-CLEAs could be repeatedly used in the batch biotransformation, and the activity retained more than 70% of the initial activity after 6 batches. These results indicated that the nitrilase-CLEA mediated dynamic kinetic resolution was a promising method for the synthesis of D-N-formyl-phenylglycine. (C) 2014 Elsevier B.V. All rights reserved.