Abstract
To improve the production of α-ketoglutaric acid (α-KG) from L-glutamate by whole-cell biocatalysis. A novel and highly active L-glutamate oxidase, SmlGOX, from Streptomyces mobaraensis was overexpressed and purified. The recombinant SmlGOX was approx. 64kDa by SDS-PAGE. SmlGOX had a maximal activity of 125±2.7 U mg-1 at pH 6.0, 35 oC. The apparent Km and Vmax values of SmlGOX were 9.3±0.5mM and 159±3 U mg-1, respectively. Subsequently, a co-expression plasmid containing the SmlGOX and KatE genes was constructed to remove H2O2, and the protein levels of SmlGOX were improved by codon optimization. Finally, by optimizing the whole-cell transformation conditions, the production of α-KG reached 77.4gl-1 with a conversion rate from L-glutamate of 98.5% after 12h. An efficient method for the production of α-KG was established in the recombinant Escherichia coli, and it has a potential prospect in industrial application.
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