Malic enzyme mutant and application thereof

By identifying potential mutation sites of malic acid oxidase using a large protein language model, we achieved highly efficient catalysis by the M144I+Q253I+T327F mutant, which solved the problems of low efficiency and insufficient stability of existing malic acid oxidases and improved the efficiency of CO2 fixation for L-malic acid synthesis.

CN121991907APending Publication Date: 2026-05-08HEFEI MICRO ERA DIGITAL TECH CO LTD
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Patent Information

Application Number
CN202610091719.3
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2026-01-22
Publication Date
2026-05-08

AI Technical Summary

Technical Problem

Existing malicases have low efficiency and insufficient environmental stability in catalyzing the synthesis of L-malic acid from CO2 fixation, making them difficult to apply in complex production systems.

Method used

Zero-sample prediction using a protein big language model identified and realized 118 potential mutation sites for malic acid oxidase. The triple mutation M144I+Q253I+T327F significantly improved the enzyme's catalytic activity and environmental adaptability.

Benefits of technology

It significantly improved the catalytic efficiency of malic acid oxidase, increasing catalytic activity by 46% and substrate affinity by 43.5%, thus expanding its application prospects in industrial production.

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Abstract

The invention relates to the technical field of enzyme engineering, in particular to a malic enzyme mutant and application thereof. Specifically, the malic enzyme derived from Escherichia coli is subjected to site mutation screening, and results show that after methionine at the 144th site is mutated into isoleucine (M144I), glutamine at the 253rd site is mutated into isoleucine (Q253I), and threonine at the 327th site is mutated into phenylalanine (T327F), the catalytic efficiency and the catalytic activity are obviously improved, which is of great significance to industrial application.
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