Kang_2016_Biotechnol.Lett_38_1009

OBJECTIVES: To characterize a novel feruloyl esterase from Escherichia coli BL21 DE3.
RESULTS: The gene encoding BioH was cloned and overexpressed in E. coli. The protein was purified and its catalytic activity was assessed. BioH exhibited feruloyl esterase activity toward a broad range of substrates, and the corresponding kinetic constants for the methyl ferulate, ethyl ferulate, and methyl p-coumarate substrates were: K m values of 0.48, 6.3, and 1.9 mM, respectively, and k cat /K m values of 9.3, 3.8, and 3.8 mM(-1) s(-1), respectively.
CONCLUSIONS: Feruloyl esterase from E. coli was expressed for the first time. BioH was confirmed to be a feruloyl esterase.