Glucose oxidase mutant

Abstract

The invention relates to the technical field of protein engineering, in particular to a glucose oxidase mutant. The glucose oxidase three-point mutant GOD-K has residual enzyme activity of 68.20% after processing at 70 DGE C for 2.5 min, after treatment at 75 DEG C for 2.5 min, the residual enzyme activity is 42.76%, which are 19.3% and 38.1% higher than that of the two point mutant GOD11, respectively. The results showed that the mutant GOD11 had unexpected effect and was more suitable for application in industrial production, so its market prospect was broad.

Description

technical field

[0001] The invention relates to the technical field of protein engineering, in particular to a glucose oxidase mutant and application thereof. Background technique

[0002] Glucose oxidase (glucose oxidase, E.C.1.1.3.4, GOD) can specifically catalyze β-D-glucose to generate gluconic acid and hydrogen peroxide under aerobic conditions. Glucose oxidase is a homodimeric molecule containing two flavin adenine dinucleotide (FAD) binding sites. Each monomer contains two completely different domains: one is non-covalently but tightly bound to part of FAD, mainly for acoustic folding; the other binds to the substrate β-D-glucose, and is supported by 4 α-helices for a trans Parallel beta-sheets.

[0003] Glucose oxidase is widely distributed in animals, plants and microorganisms. However, the content of glucose oxidase in animal and plant tissues is limited, and microorganisms are widely used as the source of glucose oxidase because of their advantages such as wide...