A dextranase mutant with improved thermal stability and high catalytic activity and its application
By performing amino acid point mutation on β-glucanase, the obtained glucanase mutant M3 remains highly viable at high temperature, solving the problem of insufficient thermal stability of existing enzymes, significantly improving catalytic vitality, and having wide industrial application potential.
CN118910012BActive Publication Date: 2025-05-27NANNING HARWORLD BIOLOGICAL TECH CORP
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Patent Information
- Application Number
- CN202411071875.0
- Authority / Receiving Office
- CN · China
- Patent Type
- Patents(China)
- Current Assignee / Owner
- Filing Date
- 2024-08-06
- Publication Date
- 2025-05-27
- Estimated Expiration
- 2044-08-06
AI Technical Summary
Technical Problem
The existing β-glucanases are insufficient thermal stability under high temperature conditions, making it difficult to meet the needs of industrial applications.
Method used
The amino acid point mutation of glucanase is performed through enzyme engineering technology to obtain the glucanase mutant M3 with high catalytic vitality and improved thermal stability. The mutant maintains high enzyme activity at high temperatures above 50°C and exhibits high activity at acidic and neutral pH.
Benefits of technology
The thermal stability of the mutant M3 at high temperatures has been significantly improved, and its catalytic vitality has been significantly improved. It can meet the needs of high-temperature environments such as the feed industry and show huge application potential.
✦ Generated by Eureka AI based on patent content.
Abstract
The present invention discloses a dextranase mutant with improved thermal stability and high catalytic activity and its application, belonging to the technical field of enzyme engineering. The amino acid sequence of the dextranase mutant M3 with improved thermal stability disclosed by the present invention is shown in SEQ ID NO.10. The high-catalytic-activity dextranase mutant disclosed by the present invention is obtained by point mutation of the amino acids of the wild-type dextranase. This mutant can withstand high-temperature treatment above 50 °C and has very high enzyme activity under acidic and neutral pH values. In particular, it has good application potential in industrial fields such as feed, beer brewing, and food.
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