Hydrophilic pet depolymerase mutant and use thereof

By introducing a specific amino acid R mutation into PETase and optimizing fermentation conditions, the problems of low PETase expression efficiency and inclusion body formation were solved, enabling the efficient and economical expression and application of PET depolymerase mutants in different hosts.

CN121574959BActive Publication Date: 2026-03-27NANJING TECH UNIV
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Patent Information

Application Number
CN202610102164.8
Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2026-01-26
Publication Date
2026-03-27
Estimated Expiration
2046-01-26

AI Technical Summary

Technical Problem

Existing PETases exhibit low expression efficiency and are prone to forming inclusion bodies in microbial systems, resulting in limited recombinant protein production that cannot meet the demands of large-scale industrial applications.

Method used

By introducing precise R mutations at specific amino acid sites of PETase, a hydrophilic PET depolymerase mutant was developed, and recombinant expression vectors and strains were constructed to optimize fermentation conditions to improve the expression level of soluble proteins and reduce inclusion body formation.

Benefits of technology

This improved the soluble expression level and enzyme activity of PETase, reduced production costs, and enabled efficient expression in Escherichia coli, Bacillus subtilis, and Pichia pastoris, thereby enhancing the economics and catalytic efficiency of industrial applications.

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Abstract

The present application relates to the field of genetic engineering and biological enzyme depolymerization of PET plastics, and particularly relates to a hydrophilic PET depolymerase mutant and application thereof. The present application obtains a hydrophilic PET depolymerase mutant V68R, or A137R or I243R by mutating the 68th, or 137th, or 243th amino acid residue of the PETase protein amino acid sequence into R. Compared with the wild-type PETase protein, under the premise of ensuring the depolymerization efficiency of PET / BHET and effectively depolymerizing PET / BHET, the expression level of soluble protein is improved, and the formation of inclusion bodies is reduced in the expression system of Escherichia coli, Bacillus subtilis or Pichia pastoris, which has economic feasibility, PETase high-yield universality, and wide application prospect.
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