کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
49600 | 46756 | 2014 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Efficient asymmetric synthesis of d-N-formyl-phenylglycine via cross-linked nitrilase aggregates catalyzed dynamic kinetic resolution Efficient asymmetric synthesis of d-N-formyl-phenylglycine via cross-linked nitrilase aggregates catalyzed dynamic kinetic resolution](/preview/png/49600.png)
• The nitrilase-CLEA was successfully prepared with activity recovery of 45.6%.
• The nitrilase-CLEA showed good stability under various conditions.
• d-N-formyl-phenylglycine was obtained with yield of 95% and 97% ee.
• The nitrilase-CLEA could be reused for 6 batches without dramatic yield loss.
In this study, a nitrilase-CLEA mediated dynamic kinetic resolution for the asymmetric synthesis of d-N-formyl-phenylglycine 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.
Figure optionsDownload as PowerPoint slide
Journal: Catalysis Communications - Volume 51, 5 June 2014, Pages 19–23