Protein glutaminase mutant with improved thermal stability and application thereof

By performing specific amino acid mutations on the parent sequence of protein glutaminase, its stability and enzyme activity at high temperatures were improved, overcoming the application limitations of wild-type enzymes in high-temperature environments, and making it suitable for food processing and feed production.

CN121574969APending Publication Date: 2026-02-27JIANGNAN UNIV
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Patent Information

Application Number
CN202511896975.1
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2025-12-16
Publication Date
2026-02-27

AI Technical Summary

Technical Problem

Wild-type protein glutaminase has poor thermal stability, which limits its application in high-temperature processing environments.

Method used

The parent sequence of protein glutaminase was modified by mutating amino acids at positions 30 and 108, including mutating serine at position 30 to phenylalanine or glutamine, and mutating serine at position 108 to glycine, alanine, methionine, threonine, aspartic acid, or glutamine. The resulting mutants showed higher thermal stability.

Benefits of technology

The mutant showed a 436.4% increase in residual enzyme activity at 60℃ compared to the wild type, and an 18.5% increase in the degree of deamidation of soybean protein at 55℃ compared to the wild type, significantly improving thermal stability and meeting the needs of high-temperature environments in industrial production.

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Abstract

The invention provides a protein glutaminase mutant with improved thermal stability and application thereof, and relates to the technical field of enzyme engineering. According to the invention, a female parent sequence of protein glutaminase is modified, the modification comprises saturated mutation and combinatorial mutation of 30th serine and 108th serine with the female parent sequence such as SEQ ID NO.1, the relative enzyme activity of the screened mutant and the residual enzyme activity after treatment at 60 DEG C are obviously improved compared with those of a wild type, and the mutant shows higher thermal stability. The residual enzyme activity of the combined mutant S30F / S108Q at the temperature of 60 DEG C is improved by 436.4% compared with that of a wild type, the deamidation degree of the combined mutant S30F / S108Q to soybean protein at the temperature of 55 DEG C is improved by 18.5% compared with that of the wild type, the problems that in the prior art, the thermal stability of protein glutaminase is poor, and industrial production and application cannot be met are solved, and the combined mutant S30F / S108Q has good application prospects in the fields of food processing, feed production and the like.
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