Efficient asymmetric synthesis of d-N-formyl-phenylglycine via cross-linked nitrilase aggregates catalyzed dynamic kinetic resolution
•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.
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Journal: Catalysis Communications - Volume 51, 5 June 2014, Pages 19–23