Identification of a Novel Dehydrogenase from Gluconobacter oxydans for Degradation of Inhibitors Derived from Lignocellulosic Biomass

نویسندگان

چکیده

Inhibitors from lignocellulosic biomass have become the bottleneck of biorefinery development. Gluconobacter oxydans DSM2003 showed a high performance inhibitors degradation, which had short lag time in non-detoxified corn stover hydrolysate and could convert 90% aldehyde to weaker toxic acids. In this study, an dehydrogenase gene W826-RS0111485, plays important function conversion DSM2003, was identified. W826-RS0111485 found by protein profiling, then series enzymatic properties were determined heterologously expressed E. coli. The results indicated that NADP is most suitable cofactor enzyme when inhibitor substrate, it highest oxidation activity furfural among several inhibitors. Under optimal reaction conditions (50 °C, pH 7.5), Km Vmax under stress 2.45 80.97, respectively, Kcat 232.22 min−1. biodetoxification experiments recombinant coli containing target completely converted 1 g/L furoic acid within 8 h, while control only 18% h. It further demonstrated played role detoxification furfural. mining degradation provide theoretical basis for rational modification industrial strains enhance its capacity future.

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ژورنال

عنوان ژورنال: Fermentation

سال: 2023

ISSN: ['2311-5637']

DOI: https://doi.org/10.3390/fermentation9030286