Mutant enzyme combination, gene, recombinant plasmid, spermidine directed synthesis bacteria and application

By performing site-directed mutagenesis on carboxysemine dehydrogenase and carboxysemine decarboxylase to form a mutant enzyme combination and constructing a two-strain co-culture system, the problem of insufficient catalytic efficiency of carboxysemine dehydrogenase and carboxysemine decarboxylase was solved, achieving efficient conversion of butanediamine and high yield of spermine.

CN122465903BActive Publication Date: 2026-09-04苏州聚维元创生物科技有限公司
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Patent Information

Application Number
CN202610920996.0
Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2026-06-25
Publication Date
2026-09-04
Estimated Expiration
2046-06-25

AI Technical Summary

Technical Problem

In the existing technology, the catalytic efficiency and continuous reaction matching of carboxysemine dehydrogenase and carboxysemine decarboxylase in the aspartic semialdehyde-butanediamine pathway are insufficient, leading to the accumulation of butanediamine, inhibiting cell activity and limiting spermidine yield and conversion efficiency.

Method used

By mutating the carboxysaminoglycan dehydrogenase from Vibrio alginolyticus to F158A and/or D262E, and the carboxysaminoglycan decarboxylase from Herminium arsenogenis to L270A, a mutant enzyme combination was formed, improving the enzyme's substrate binding ability and catalytic efficiency. A two-strain co-culture system was constructed to achieve the efficient conversion of butanediamine to spermine.

Benefits of technology

It significantly reduces butylene diamine accumulation, increases spermidine production rate and synthesis yield, weakens the cytotoxic inhibitory effect of butylene diamine, promotes the dynamic balance between precursor supply and product synthesis, and improves spermidine yield and conversion efficiency.

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Abstract

The application discloses a mutant enzyme combination, genes, a recombinant plasmid, spermidine directed synthesis bacteria and application, and relates to the technical field of biological engineering. A carboxyspermidine dehydrogenase mutant of the mutant enzyme combination is subjected to amino acid mutation on the basis of an amino acid sequence shown in SEQ ID NO:1, the amino acid mutation is single-point mutation or combined mutation of F158A and D262E, and a carboxyspermidine decarboxylase mutant is subjected to amino acid mutation on the basis of an amino acid sequence shown in SEQ ID NO:2, the amino acid mutation is single-point mutation of L270A. The mutant enzyme combination is formed by the carboxyspermidine dehydrogenase mutant and the carboxyspermidine decarboxylase mutant through specific site mutation, the catalytic efficiency and reaction matching of continuous conversion of butanediamine and aspartic acid semialdehyde to spermidine are improved, thereby butanediamine accumulation is reduced, and the yield and conversion efficiency of spermidine are improved.
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