Glucose oxidase mutants with improved thermostability and acid tolerance and antibacterial applications thereof

By performing site-directed mutagenesis on glucose oxidase, its thermal stability and acid tolerance were improved while maintaining high catalytic activity, solving the problem of decreased enzyme activity in existing technologies and enabling efficient application in acidic environments.

CN120485144BActive Publication Date: 2026-07-07AFFILIATED HOSPITAL OF JIANGSU UNIV
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
AFFILIATED HOSPITAL OF JIANGSU UNIV
Filing Date
2025-05-16
Publication Date
2026-07-07

AI Technical Summary

Technical Problem

Existing technologies struggle to maintain catalytic activity while improving the thermal stability and acid tolerance of glucose oxidase, and traditional modification strategies often result in a decrease in enzyme activity.

Method used

By site-directed mutagenesis of key amino acid sites Glu148 and Phe283 in glucose oxidase from Aspergillus, which were transformed into Lys148 and Tyr283 respectively, recombinant strains were constructed, and glucose oxidase mutants AiGODL_E148K/F283Y with improved heat stability and acid tolerance were screened out.

Benefits of technology

The mutant AiGODL_E148K/F283Y exhibits a 5°C increase in optimal temperature, a 9°C increase in T50 value, and a 12-minute increase in half-life at 70°C. It also demonstrates improved pH tolerance with 19%-74% increased enzyme activity in acidic environments, showing great promise for antibacterial and antibiotic alternative applications.

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Abstract

The application discloses a glucose oxidase mutant with simultaneously improved thermal stability and acid resistance and antibacterial application thereof, and belongs to the field of genetic engineering and protein engineering. The application takes glucose oxidase AiGODL as a mother to obtain a mutant AiGODL_E148K / F283Y by respectively mutating Glu148 and Phe283 into Lys148 and Tyr283. It is found through experiments that, compared with wild-type glucose oxidase AiGODL, the mutant AiGODL_E148K / F283Y has improved heat resistance and acid resistance, and has the same level of specific activity and catalytic efficiency as AiGODL and the same antibacterial performance as ampicillin. The mutant AiGODL_E148K / F283Y provided by the application has great application prospect in antibacterial and antibiotic substitution.
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