Discovery of novel feruloyl esterase activity of BioH in Escherichia coli BL21(DE3)

To characterize a novel feruloyl esterase from Escherichia coli BL21 DE3. 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. Feruloyl esterase from E. coli was expressed for the first time. BioH was confirmed to be a feruloyl esterase.