Discovery and Biochemical Characterization of a Methanol Dehydrogenase From Lysinibacillus xylanilyticus.

ABSTRACT: Bioconversion of C1 chemicals such as methane and methanol into higher carbon-chain chemicals has been widely studied. Methanol oxidation catalyzed by methanol dehydrogenase (Mdh) is one of the key steps in methanol utilization in bacterial methylotrophy. In bacteria, few NAD⁺-dependent Mdhs have been reported that convert methanol to formaldehyde. In this study, an uncharacterized Mdh gene from Lysinibacillus xylanilyticus (Lxmdh) was cloned and expressed in Escherichia coli. The maximum alcohol oxidation activity of the recombinant enzyme was observed at pH 9.5 and 55°C in the presence of 10 mM Mg²⁺. To improve oxidation activity, rational approach-based, site-directed mutagenesis of 16 residues in the putative active site and NAD⁺-binding r

SUBMITTER: Lee JY 

PROVIDER: S-EPMC7033420 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature