Efficient expression of Streptomyces mobaraensis transglutaminase in Escherichia coli

  • YUAN Fang ,
  • LI Guoying ,
  • GU Qiuya ,
  • YU Xiaobin
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  • 1(School of Biotechnology, Jiangnan University, Wuxi 214122, China)
    2(Jiangsu Yiming Biological Technology Co. Ltd., Taixing 225400, China)

Received date: 2024-03-15

  Revised date: 2024-04-25

  Online published: 2025-03-28

Abstract

Transglutaminase (TGase) can promote intramolecular or intermolecular cross-linking of proteins, and is widely used in food, pharmaceutical, textile, and other industries.In order to efficiently produce TGase with excellent properties, two TGases from Streptomyces mobaraensis were investigated in this study.The properties of two TGases from different strains were investigated, and the TGase gene tgLD with excellent properties was heterologously expressed in Escherichia coli using six different plasmids, respectively.Mature TGase was successfully expressed in the recombinant E.coli BL21(DE3) (pET32a-tgLD).The activity of recombinant TGLD reached 0.45 U/mL after 8 h induction using 0.2 mmol/L IPTG at 25 ℃.In order to further improve the expression level of TGLD, two recombinant strains were constructed to specifically activate pro-TGase, respectively.The activity of TGLD in recombinant E.coli BL21(DE3) (pCOLDII-pro-EK-tgLD) after activation in vitro reached 25.23 U/mL after 24 h induction using 0.2 mmol/L IPTG at 15 ℃.Activated TGLDwith excellent properties were efficiently expressed in E.coli in this study.

Cite this article

YUAN Fang , LI Guoying , GU Qiuya , YU Xiaobin . Efficient expression of Streptomyces mobaraensis transglutaminase in Escherichia coli[J]. Food and Fermentation Industries, 2025 , 51(5) : 61 -69 . DOI: 10.13995/j.cnki.11-1802/ts.039235

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