Enzymatic Synthesis of Tyrosinase Mutants, Immobilized Enzymes, and 5,6-Dihydroxyindole

By using tyrosinase mutants with specific amino acid sequence mutations and immobilized enzyme technology, the problems of low purity and safety in DHI synthesis have been solved, enabling the production of efficient and environmentally friendly hair dye alternatives.

CN122128257BActive Publication Date: 2026-07-17HUNAN FLAG BIOTECHNOLOGY CO LTD
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
HUNAN FLAG BIOTECHNOLOGY CO LTD
Filing Date
2026-04-30
Publication Date
2026-07-17

AI Technical Summary

Technical Problem

Aromatic amines in existing hair dyes pose significant health risks, and the synthesis process of 5,6-dihydroxyindole (DHI) is difficult to control for side reactions, resulting in low product purity and making it difficult to overcome the bottlenecks in mass production technology.

Method used

By using tyrosinase mutants with specific amino acid sequence mutations and combining them with immobilized enzyme technology, DHI is synthesized through enzyme catalysis. The reaction conditions are optimized using divalent transition metal ions and enhancers to achieve continuous enzyme-catalyzed synthesis.

Benefits of technology

This improved the reaction conversion rate and stability of DHI, reduced production costs, and enabled the production of efficient and environmentally friendly hair dye alternatives.

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Abstract

This invention belongs to the field of enzyme catalysis. It discloses a tyrosinase mutant, an immobilized enzyme, and an enzymatically catalyzed synthesis method for 5,6-dihydroxyindole. The amino acid sequence of the tyrosinase mutant is a sequence containing at least one mutation from R209H, F197W, T17P, or Q187L in the wild-type amino acid sequence shown in SEQ ID NO.1. Research in this invention shows that by mutating the specific sites mentioned above in the wild-type sequence of SEQ ID NO.1, the catalytic activity of the enzyme can be significantly enhanced. Using this enzyme in the catalytic synthesis of 5,6-dihydroxyindole can effectively improve the reaction conversion rate.
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