Chemical Research in Chinese Universities ›› 2014, Vol. 30 ›› Issue (2): 289-292.doi: 10.1007/s40242-014-3401-y

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Enzymatic Promiscuity:Escherichia coli BioH Esterase-catalysed Aldol Reaction and Knoevenagel Reaction

JIANG Ling, YU Hongwei   

  1. Department of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310007, P. R. China
  • Received:2013-09-24 Revised:2013-12-27 Online:2014-04-01 Published:2014-01-13
  • Contact: YU Hongwei E-mail:yuhongwei@zju.edu.cn
  • Supported by:

    Supported by the National Natural Science Foundation of China(No.21176215).

Abstract:

Esterase BioH, which is obligatory for biotin synthesis in Escherichia coli, was found to exhibit a promiscuous ability to catalyse Aldol and Knoevenagel reactions with moderate to good yields. The reaction conditions including organic solvent, molar ratio of ketone to aldehyde, enzyme amount, and reaction time were investigated to evaluate the effect of different reaction conditions on yield. Target compounds were afforded in the best yield of 91.2% for Aldol reaction and 54.7% for Knoevenagel reaction. In addition, because the enzyme could be prepared with a low cost, this protocol could provide an economic route to conduct Aldol and Knoevenagel reactions, which expand the field of enzymatic promiscuity.

Key words: Escherichia coli BioH esterase, Catalytic promiscuity, Aldol reaction, Knoevenagel reaction