Abstract
Ten lipases and esterases have been examined to catalyse the reaction between p-nitrobenzaldehyde and methyl vinyl ketone, the Baylis–Hillman reaction, to form 3-[hydroxyl-(4-nitrophenyl)-methyl]-but-3-en-2-one. Among these enzymes, Escherichia coli BioH esterase had the best activity. Optimal conditions for this reaction were: 0.1 mmol aldehyde, 0.1 mmol activated alkene, 30 mg E. coli BioH, 1 ml acetonitrile at 30 °C for 96 h. In addition to the named substrates, four other aldehydes and three activated alkenes were also investigated to determine the substrate range of the enzyme. The structures of nine products were confirmed by NMR and yields of the corresponding products ranged from 21 to 46 %.
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Acknowledgments
This work is financially supported by the National Natural Science Foundation of China (21176215/21176102), the Outstanding Young Scholar Grant of Zhejiang University (R4110092) and the Program for Zhejiang leading team of S&T Innovation (2011R50007). We thank all the members of Professor Yu’s group.
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Jiang, L., Yu, Hw. An example of enzymatic promiscuity: the Baylis–Hillman reaction catalyzed by a biotin esterase (BioH) from Escherichia coli . Biotechnol Lett 36, 99–103 (2014). https://doi.org/10.1007/s10529-013-1329-9
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DOI: https://doi.org/10.1007/s10529-013-1329-9