A method for the enzymatic synthesis of 2-(4-nitrophenyl)butyric acid, an intermediate of indobufen.

By modifying the amino acid sequence of nitrile hydrolase Gi-Nit, a highly efficient nitrile hydrolase mutant was constructed, solving the problems of harsh reaction conditions and low catalytic efficiency of nitrile hydrolase in the chemical synthesis of indobufen, and realizing the efficient and environmentally friendly synthesis of indobufen intermediates.

CN120888531BActive Publication Date: 2026-05-26PEKING UNIVERSITY THIRD HOSPITAL (THE THIRD CLINICAL MEDICAL SCHOOL OF PEKING UNIVERSITY) +2
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Patent Information

Application Number
CN202511425944.8
Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2025-09-30
Publication Date
2026-05-26
Estimated Expiration
2045-09-30

AI Technical Summary

Technical Problem

Existing chemical methods for synthesizing indobufen suffer from problems such as harsh reaction conditions, use of toxic and harmful raw materials, and difficulty in controlling impurities. Wild-type nitrile hydrolases exhibit low catalytic efficiency and low product concentration when catalyzing 2-(4-nitrophenyl)butyronitrile.

Method used

By modifying Gi-Nit, a nitrile hydrolase from Gibraltar tiglium, through protein engineering techniques and performing single- or multi-point mutations in the amino acid sequence, a highly efficient nitrile hydrolase mutant was constructed, thereby enhancing its hydrolytic activity against 2-(4-nitrophenyl)butyronitrile.

Benefits of technology

The nitrile hydrolase mutant exhibits 32-fold increased catalytic activity and 15.8-fold increased yield, providing a green and efficient basis for the synthesis of indobufen intermediates.

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Abstract

This invention belongs to the fields of enzyme engineering and biotechnology, and discloses a nitrile hydrolase mutant, its encoding gene, recombinant vector, recombinant genetically engineered bacteria, enzyme preparation, and applications. The nitrile hydrolase mutant is obtained by single-point or multi-point mutation of amino acids 8, 17, 35, or 150 of the nitrile hydrolase amino acid sequence shown in SEQ ID NO. 2. The nitrile hydrolase mutant of this invention exhibits 32-fold increased activity and 15.8-fold increased yield compared to the wild-type Gi-Nit, laying the foundation for the industrial enzymatic synthesis of 2-(4-nitrophenyl)butyric acid.
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