| Institution: | 1.The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology,Jiangnan University,Wuxi,China;2.College of Life Sciences,Northwest University,Xi’an,China |
| Abstract: | ObjectivesTo characterize a novel feruloyl esterase from Escherichia coli BL21 DE3.ResultsThe 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.ConclusionsFeruloyl esterase from E. coli was expressed for the first time. BioH was confirmed to be a feruloyl esterase. |
