Efficient production of a thermostable variant of transglutaminase in Streptomyces mobaraensis

  • ZHANG Ni ,
  • QIU Jieru ,
  • GUAN Xingzi ,
  • YE Jiacai ,
  • LIU Song
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  • 1(Science Center for Future Foods, Jiangnan University, Wuxi 214122, China)
    2(School of Biotechnology, Jiangnan University, Wuxi 214122, China)

Received date: 2024-03-07

  Revised date: 2024-05-26

  Online published: 2026-03-18

Abstract

Transglutaminase (EC 2.3.2.13 TGase) is an important industrial enzyme capable of catalyzing protein cross-linking or modification by small molecules.To enhance the fermentation level of thermostable TGase, this study expressed the thermostable mutant TGm2A in the mutant strain smY2022Δtg of Streptomyces mobaraensis and analyzed its enzymatic properties and protein cross-linking ability under high-temperature conditions.Initially, the impact of six strong promoters on TGm2A expression was evaluated, revealing that the glyceraldehyde-3-phosphate dehydrogenase promoter (Pgapdh) achieved the highest yield of TGm2A at 31.48 U/mL.Subsequently, by tandemly linking the TGase promoter (PsmY2022-2) with Pgapdh to form the promoter PsmY2022-2/gapdh, the yield of TGm2A was further increased to 64.94 U/mL.Building on this, a double-copy TGm2A strain, smY2022-TGm2A-2C, was constructed, which achieved an enzyme activity of 93.62 U/mL after 84 h of fermentation, making it the highest-yielding TGase strain reported to date.Enzymatic characterization indicated that TGm2A has a half-life of 120.36 min at 60 ℃, which is 100 times that of the wild type.Additionally, TGm2A demonstrated significantly superior cross-linking ability with β-casein at 70 ℃ compared to the wild-type TGase.This study lays the foundation for the industrial production of TGase and its application in high-temperature processing.

Cite this article

ZHANG Ni , QIU Jieru , GUAN Xingzi , YE Jiacai , LIU Song . Efficient production of a thermostable variant of transglutaminase in Streptomyces mobaraensis[J]. Food and Fermentation Industries, 2026 , 52(2) : 1 -9 . DOI: 10.13995/j.cnki.11-1802/ts.042634

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