D-allulose-3-epimerase mutant, host cell, and its application in allulose synthesis.

By performing multi-point mutations on D-allulose-3-epimerase, its catalytic activity and stability were improved, solving the problems of low catalytic activity and poor stability in existing technologies, and realizing efficient D-allulose production.

CN121065161BActive Publication Date: 2026-07-17BINZHOU SANYUAN BIOLOGICAL TECH
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
BINZHOU SANYUAN BIOLOGICAL TECH
Filing Date
2025-08-05
Publication Date
2026-07-17

AI Technical Summary

Technical Problem

Existing D-allulose-3-epimerases have limited catalytic activity, low conversion efficiency, and poor stability, making them unsuitable for the high-temperature, high-sugar, and high-ionic-strength environments of large-scale industrial production.

Method used

By performing multiple point mutations at positions 47, 72, 114, and 221 on wild-type D-allulose-3-epimerase derived from Ruminococcus CAG55, a series of D-allulose-3-epimerase mutants were developed and applied to Escherichia coli and Bacillus subtilis host cells to optimize their catalytic activity and stability.

Benefits of technology

It significantly improved the catalytic activity and stability of D-allulose-3-epimerase, with a conversion rate of 36.3% when the host bacterium was Escherichia coli and 35.5% when the host bacterium was Bacillus subtilis. Furthermore, the enzyme activity could be maintained at 80% even after 30 repeated uses after immobilization.

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Abstract

This invention discloses a D-allulose-3-epimerase mutant, its host cell, and its application in the synthesis of allulose, belonging to the field of genetic engineering technology. This invention utilizes a mutant derived from Ruminococcus CAG55 (… Ruminococcus sp. Simultaneous mutations at positions 47, 72, 114, and 221 of wild-type D-allulose-3-epimerase (CAG55) yielded a series of D-allulose-3-epimerase mutants, significantly improving their catalytic activity and stability. The mutants obtained by simultaneous mutations at positions 47, 72, 114, and 221 exhibited the highest catalytic activity. The D-allulose-3-epimerase mutants provided by this invention have significant application value in the production of D-allulose.
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