Method for enhancing synthesis capability of yeast total protein and dipeptide tripeptide

By replacing the TATA box-binding protein-coding gene in yeast, a recombinant yeast engineered strain was constructed, which solved the problem of insufficient total protein and bioactive peptide synthesis capacity in yeast in the existing technology. It achieved a significant increase in total protein content and a significant enhancement in dipeptide and tripeptide accumulation, simplified the operation process, and provided global regulatory advantages.

CN122081371APending Publication Date: 2026-05-26TIANJIN UNIV
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Patent Information

Application Number
CN202610330163.9
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2026-03-18
Publication Date
2026-05-26

AI Technical Summary

Technical Problem

Existing technologies lack methods to simultaneously and efficiently enhance the synthesis capacity of total yeast protein and bioactive peptides, and there is insufficient attention paid to the systemic changes in dipeptides and tripeptides.

Method used

By replacing the endogenous TATA box-binding protein encoding gene ScSPT15 of Saccharomyces cerevisiae with the TATA box-binding protein encoding gene YlSPT15 of Yersinia lipolytica, a recombinant yeast engineered strain was constructed to achieve global transcriptional regulation.

Benefits of technology

It significantly increased the total protein content and dipeptide and tripeptide accumulation levels in yeast, simplified the operation process, synergistically regulated multiple physiological processes, and enhanced the protein synthesis capacity and peptide metabolite library of the strain.

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Abstract

The invention discloses a method for enhancing the synthetic ability of yeast total protein and dipeptide tripeptide. Relates to the technical field of synthetic biology and metabolic engineering. According to the invention, the saccharomyces cerevisiae engineering strain with high protein synthesis capability and high endogenous dipeptide and tripeptide accumulation level is successfully constructed. The metabonomics analysis reveals the unique peptide fragment accumulation spectrum, especially the generation of a large amount of lysine-rich tripeptide at the C terminal, and proposes a potential mechanism of metabolic pathway'bottleneck 'caused by peptidase activity down-regulation in combination with proteome data. The recombinant strain has important application potential in the fields of single-cell protein, functional peptide products and the like.
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