Laccase and application thereof
By using database mining and E. coli recombinant expression technology, the amino acid sequence and nucleic acid molecule of laccase Lac-11 were optimized, solving the problems of insufficient activity and poor stability of existing laccases. This enabled efficient dye decolorization and lignin degradation, reducing the cost of industrial enzymes.
CN122012426AActive Publication Date: 2026-05-12HANGZHOU LUCA INTELLIGENT TECHNOLOGY CO LTD
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Patent Information
- Application Number
- CN202610493354.7
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Filing Date
- 2026-04-15
- Publication Date
- 2026-05-12
- Estimated Expiration
- 2046-04-15
AI Technical Summary
Technical Problem
Existing laccases suffer from insufficient activity, poor stability, and high production costs, making it difficult to meet the needs of industrial applications.
Method used
The highly active laccase candidate protein Lac-11 was obtained through database mining, and it was recombinantly expressed in E. coli and purified by affinity chromatography. By combining it with a His tag, its amino acid sequence and nucleic acid molecule were optimized to improve enzyme activity, pH and thermal stability.
Benefits of technology
Lac-11 exhibits 50% higher enzyme activity, high pH stability within the range of 5.0-8.0, excellent thermal stability within the range of 50-80℃, high dye decolorization rate, and significantly improved lignin degradation efficiency.
✦ Generated by Eureka AI based on patent content.
Abstract
The invention discloses laccase and application thereof, and belongs to the field of bioengineering. The high-activity laccase Lac-11 is obtained through database mining, and compared with existing high-activity laccase BstCotA, the high-activity laccase Lac-11 has the following beneficial effects that 1, the enzyme activity is remarkably improved, the enzyme activity is improved by nearly 50% under the conditions that the temperature is 37 DEG C and the pH is 5.0, and the industrial enzyme cost is reduced; 2, the pH stability is higher, the enzyme activity retention rate is higher in the pH range of 5.0-8.0, and the method is suitable for wider acid-base environments. And 3, the thermal stability is better, the stability at the medium-high temperature interval of 50-80 DEG C is obviously higher than that of a control enzyme, and the method is suitable for an industrial high-temperature process. 4, the dye decolorization efficiency is higher, the decolorization rates of amino black 10B and crystal violet respectively reach 31% and 37%, and printing and dyeing wastewater can be efficiently treated. And 5, the lignin degradation capacity is outstanding, the degradation rates within 1 hour, 2 hours and 24 hours are 22%, 25% and 58% respectively, and pulping bleaching and biomass recycling are facilitated.
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