A modified mannitol dehydrogenase and use thereof
By mutating the amino acid sequence of mannitol dehydrogenase and coupling it with recombinant strains, the coenzyme dependence and stability issues of MDH in biotransformation were resolved, enabling efficient and low-cost D-mannitol production.
CN121931070BActive Publication Date: 2026-07-03ZHEJIANG HUAKANG PHARMA
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Patent Information
- Application Number
- CN202610396017.6
- Authority / Receiving Office
- CN · China
- Patent Type
- Patents(China)
- Current Assignee / Owner
- Filing Date
- 2026-03-30
- Publication Date
- 2026-07-03
- Estimated Expiration
- 2046-03-30
AI Technical Summary
Technical Problem
Existing mannitol dehydrogenase (MDH) suffers from coenzyme dependence, high cost, poor stability, and low conversion efficiency in biotransformation methods, which limits its application in industrial production.
Method used
By performing specific site mutations on the amino acid sequence of mannitol dehydrogenase, including C37A, Q75V, Q176L, Q185N, E197R, F225M, Y244F, and Q300L, the enzyme activity and stability were improved. Furthermore, the transformation process was optimized by coupling recombinant strains with formate dehydrogenase.
Benefits of technology
It significantly improves the conversion rate of D-fructose to D-mannitol, reduces production costs, and enhances enzyme activity and stability, making it suitable for large-scale industrial production.
✦ Generated by Eureka AI based on patent content.
Abstract
The present application belongs to the technical field of bioengineering, and relates to a reformed mannitol dehydrogenase and application thereof As The amino acid sequence of the MDH is shown in SEQ ID NO. 1, and the amino acid mutation is at least one of positions 37, 75, 176, 185, 197, 225, 244 and 300. Cb The strain containing the formic acid dehydrogenase of the FDH plasmid is coupled with the strain containing the mannitol dehydrogenase, and then the efficiency of producing D-mannitol from D-fructose is significantly improved. After adding 150 g / L of fructose for 8 h, the conversion rate of the double-enzyme system of the recombinant strain containing the Y224F mutant reaches 90.12%, and the conversion rate of the double-enzyme system of the recombinant strain containing the Q300L mutant reaches 86.23%. The present application reduces the cost of the recombinant strain, improves the enzyme activity, and improves the conversion efficiency of D-mannitol.
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