A mutant capable of catalyzing demethylation of ferulic acid to prepare caffeic acid and application thereof

By site-directed mutagenesis of the alpha subunit of vanillic acid demethylase and its expression in Escherichia coli, the technical challenge of preparing caffeic acid from ferulic acid demethylation was solved, realizing the green and efficient preparation of caffeic acid from lignocellulosic biomass, and providing a new method for the high-value utilization of agricultural and forestry waste.

CN122256278APending Publication Date: 2026-06-23INST OF COTTON RES CHINESE ACAD OF AGRI SCI
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
INST OF COTTON RES CHINESE ACAD OF AGRI SCI
Filing Date
2026-04-30
Publication Date
2026-06-23

AI Technical Summary

Technical Problem

The lack of existing bio-enzymes that can directly catalyze the demethylation of ferulic acid to produce caffeic acid makes caffeic acid extraction difficult and expensive, and the abundant ferulic acid in lignocellulose biomass has not been effectively utilized.

Method used

By site-directed mutagenesis of the alpha subunit of wild-type vanillic acid demethylase, particularly modifying glutamine at position 167, aspartic acid at position 171, and lysine at position 168, a mutant capable of catalyzing the demethylation of ferulic acid to produce caffeic acid was designed. This enzyme was then expressed in Escherichia coli, and ferulic acid was obtained by alkali-catalyzed treatment of lignocellulose biomass.

Benefits of technology

This study achieves efficient and green preparation of caffeic acid from lignocellulose biomass, avoiding high-temperature and high-pressure reactions and the use of additional catalysts, and provides a new way to utilize agricultural and forestry waste for high value.

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Abstract

The application provides a mutant capable of catalyzing demethylation of ferulic acid to prepare caffeic acid and an application thereof, and belongs to the technical field of biological catalysis. The mutant provided by the application has at least one mutation compared with wild-type vanillin demethylase alpha subunit, and the mutations are as follows: (1) glutamine at the 167th position is mutated into alanine, histidine, serine or glycine; (2) aspartic acid at the 171st position is mutated into alanine, histidine or glycine; (3) lysine at the 168th position is mutated into alanine. The mutant provided by the application can catalyze demethylation of ferulic acid to prepare caffeic acid, is green and sustainable, has no pollutants generated in the conversion process, is simple to operate, does not need to add an additional catalyst, and does not involve a high-temperature and high-pressure reaction. Moreover, ferulic acid is derived from lignocellulosic biomass, the lignocellulosic biomass is widely sourced, the raw material is sustainable, and a new way is provided for high-value utilization of agricultural and forestry waste.
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