A higher molecular species observed for the recombinant LGOX was not detected for the Sgmp-treated recombinant LGOX. Furthermore, the Sgmp-treated recombinant LGOX had a subunit structure of α 2β 2γ 2 and nearly the same enzymological character as the LGOX isolated from Streptomyces sp. Proteolysis of the recombinant LGOX with the metalloendopeptidase from Streptomyces griseus (Sgmp) improved its catalytic efficiency at various pH. The recombinant LGOX exhibited low thermostability compared to the LGOX isolated from Streptomyces sp.
Although the recombinant LGOX exhibited catalytic activity, it was inferior to the LGOX isolated from Streptomyces sp. coli transformant had the structure of a one chain polypeptide. The gene encoding LGOX was cloned and heterologously expressed in Escherichia coli. X-119-6 is a protein of 150 kDa that has hexamer structure α 2β 2γ 2. L-Glutamate oxidase (LGOX) from Streptomyces sp.
