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The gene encoding glucose oxidase from  Aspergillus niger  ZM-8 was cloned and transferred to  Pichia pastoris  GS115, a transgenic strain  P. pastoris  GS115-His-GOD constructed. The growth curve of  P. pastoris  GS115-His-GOD was consistent with that of  Pichia pastoris GS115 -pPIC9K under non-induced culture conditions. Under methanol induction conditions, the growth of the GOD-transgenic strain was significantly lowered than  P. pastoris  GS115-pPIC9K with the induced-culture time increase, and the optical densities of GOD-transgenic strain reached one-third of that of the  P. pastoris  GS115-pPIC9K at 51 h. The activity of glucose oxidase in the cell-free supernatant, the supernatant of cell lysate, and the precipitation of cell lysate was 14.3 U/mL, 18.2 U/mL and 0.48 U/mL, respectively. The specific activity of glucose oxidase was 8.3 U/mg, 6.52 U/mg and 0.73 U/mg, respectively. The concentration of hydrogen peroxide formed by glucose oxidase from supernatant of the fermentation medium, the supernatant of the cell lysate, and the precipitation of cell lysate catalyzing 0.2 M glucose was 14.3 μg/mL, 18.2 μg/mL, 0.48 μg/mL, respectively. The combination of different concentrations of glucose oxidase and glucose could significantly inhibit the growth of  Agrobacterium  and  Escherichia coli  in logarithmic phase. The filter article containing supernatant of the fermentation medium, supernatant of the cell lysate, and precipitation of cell lysate had no inhibitory effect on  Agrobacterium  and  E. coli . The minimum inhibitory concentration of hydrogen peroxide on the plate culture of  Agrobacterium  and  E. coli  was 5.6 × 10 3  μg/mL and 6.0 × 10 3  μg/mL, respectively.

peerj

Expression of Aspergillus niger glucose oxidase in Pichia pastoris and its antimicrobial activity against Agrobacterium and Escherichia coli