一种7α-羟基类固醇脱氢酶突变体及其应用
By directionally modifying 7α-hydroxysteroid dehydrogenase and mutating the amino acid sites V96T, D152K, and F204Y, the problems of thermostability and product inhibition of the wild-type enzyme were solved, and more efficient preparation of 7-KLCA or T-7-KLCA was achieved, which is suitable for industrial production.
Patent Information
- Authority / Receiving Office
- CN · China
- Patent Type
- Patents(China)
- Current Assignee / Owner
- HUNAN FLAG BIOTECHNOLOGY CO LTD
- Filing Date
- 2022-07-19
- Publication Date
- 2026-07-17
AI Technical Summary
Wild-type 7α-hydroxysteroid dehydrogenases suffer from low specific activity, poor thermal stability, and severe product feedback inhibition when preparing taurine-7-ketolithocholic acid (T-7-KLCA) or 7-ketolithocholic acid (7-KLCA), resulting in poor yields that cannot meet the needs of industrial applications.
7α-hydroxysteroid dehydrogenase derived from Clostridium absonum was modified using directed evolution technology. The mutant amino acid sites included V96T, D152K, and F204Y, resulting in a mutant enzyme with better thermal stability, higher catalytic activity, and weaker product inhibition.
The mutant enzyme exhibits higher specific activity, better thermal stability, and lower product inhibition when catalyzing the preparation of 7-KLCA or T-7-KLCA, with a shorter reaction time, meeting the needs of industrial applications.
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Figure CN115927225B_ABST