Journal of Microbiology and Biotechnology

  • 제30권7호
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  • Pages.1082-1091
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  • 2020
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
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Heterologous Expression of Recombinant Transglutaminase in Bacillus subtilis SCK6 with Optimized Signal Peptide and Codon, and Its Impact on Gelatin Properties

  • Wang, Shiting (Key Laboratory of Leather Chemistry and Engineering (Sichuan University), Ministry of Education) ;
  • Yang, Zhigang (Chengdu Jinkai Bioengineering Co., Ltd.) ;
  • Li, Zhenjiang (Chengdu Jinkai Bioengineering Co., Ltd.) ;
  • Tian, Yongqiang (Key Laboratory of Leather Chemistry and Engineering (Sichuan University), Ministry of Education)
  • 투고 : 2020.02.26
  • 심사 : 2020.04.19
  • 발행 : 2020.07.28
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초록

Microbial transglutaminases (MTGs) are widely used in the food industry. In this study, the MTG gene of Streptomyces sp. TYQ1024 was cloned and expressed in a food-grade bacterial strain, Bacillus subtilis SCK6. Extracellular activity of the MTG after codon and signal peptide (SP Ync M) optimization was 20 times that of the pre-optimized enzyme. After purification, the molecular weight of the MTG was 38 kDa and the specific activity was 63.75 U/mg. The optimal temperature and pH for the recombinant MTG activity were 50℃ and 8.0, respectively. MTG activity increased 1.42-fold in the presence of β-ME and 1.6-fold in the presence of DTT. Moreover, 18% sodium chloride still resulted in 83% enzyme activity, which showed good salt tolerance. Cross-linking gelatin with the MTG increased the strength of gelatin 1.67 times and increased the thermal denaturation temperature from 61.8 to 75.8℃. The MTG also significantly increased the strength and thermal stability of gelatin. These characteristics demonstrated the huge commercial potential of MTG, such as for applications in salted protein foods.

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피인용 문헌

  1. An overview and future prospects of recombinant protein production in Bacillus subtilis vol.105, pp.18, 2020, https://doi.org/10.1007/s00253-021-11533-2