Carbonyl reductase mutants and their use in the preparation of (r)-8-chloro-6-hydroxyoctanoate compounds
By modifying the carbonyl reductase mutant of Pichia pastoris and co-expressing it with glucose dehydrogenase, the problem of low enzyme activity and efficiency in the enzymatic preparation of (R)-8-chloro-6-hydroxyoctanoate compounds was solved, and efficient and low-cost catalytic synthesis was achieved.
CN115948356BActive Publication Date: 2026-01-06FUDAN UNIVERSITY
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Patent Information
- Application Number
- CN202111167493.4
- Authority / Receiving Office
- CN · China
- Patent Type
- Patents(China)
- Current Assignee / Owner
- Filing Date
- 2021-10-07
- Publication Date
- 2026-01-06
- Estimated Expiration
- 2041-10-07
AI Technical Summary
Technical Problem
Existing enzymatic methods for preparing (R)-8-chloro-6-hydroxyoctanoate compounds suffer from problems such as insufficient enzyme activity, low reaction efficiency, high coenzyme dosage, and high cost.
Method used
Through enzyme library screening and protein engineering, a carbonyl reductase mutant derived from Pichia pastoris was developed and co-expressed with glucose dehydrogenase to improve its catalytic properties for the efficient synthesis of (R)-8-chloro-6-hydroxyoctanoate compounds.
Benefits of technology
It improves the catalytic activity and stereoselectivity of carbonyl reductase, reduces the amount of coenzyme required, simplifies the operation process, and is suitable for industrial production.
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Abstract
The application discloses a carbonyl reductase mutant and application thereof in preparation of (R)-8-chloro-6-hydroxyoctanoate compounds. The application relates to a mutant of carbonyl reductase with improved catalytic performance and stereoselectivity after rational molecular modification, a recombinant expression plasmid containing the mutant gene of the enzyme, a recombinant expression transformant, a preparation method of the recombinant enzyme, and application of the recombinant enzyme or the recombinant cell as a catalyst in asymmetric reduction of 8-chloro-6-carbonyloctanoate compounds (I) to prepare (R)-8-chloro-6-hydroxyoctanoate compounds (II), in particular, in an intermediate (R)-8-chloro-6-hydroxyoctanoate methyl ester of thioctic acid. The disclosed carbonyl reductase SsCR mutant has the advantages of high reaction efficiency and high catalytic activity, and exhibits the advantages of high substrate concentration, low catalyst consumption and short reaction time in the process of catalytic preparation of the compound (II).
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