The Korean Journal of Mycology (한국균학회지)

The Korean Society of Mycology (한국균학회)
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Expression and Cloning of Microbial Transglutaminase in S. cerevisiae

세균 유래 단백질연결효소 Transglutaminase의 클로닝과 효모에서의 발현

  • Kim, Hyoun-Young (Institute of Basic and Natural Science, Woosuk University) ;
  • Oh, Dong-Soon (Department of Pharmaceutical Engineering, Woosuk University) ;
  • Kim, Jong-Hwa (Department of Pharmaceutical Engineering, Woosuk University)
  • 김현영 (우석대학교 기초과학연구소) ;
  • 오동순 (우석대학교 제약공학과) ;
  • 김종화 (우석대학교 제약공학과)
  • Published : 2008.06.30
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Abstract

A $Ca^{2+}-independent$ microbial transglutaminase (mTGase) from the actinomycete Streptomyces mobaraensis IFO13819 is a useful enzyme in the food industry. It is consists 406 amino acid residues, which comprised leader and pro region of 75 amino acid residues and the structure region of 331 amino acid residues. Pro and structure gene of TGase were cloned into the yeast shuttle vector pYAEG-TER and then used to transform Saccharomyces cerevisiae 2805. Expression of mTGase in recombinant was confirmed with Northern hybridization and the maximal activity of TGase was shown 26 mU/ml.

방선균 Streptomyces mobaraensis IFO13819 유래 transglutaminase(mTGase)는 칼슘 비의존성으로 식품산업에서 유용하게 이용되고 있는 효소이다. mTGase는 406개의 아미노산으로 구성되어 있는데 leader와 pro 부위는 75개, 구조 부위는 331개의 아미노산으로 구성되어있다. mTGase의 pro와 구조 유전지를 pYAEG-TER 벡터에 클로닝하고 Saccharomyces cerevisiae 2805에 형질전환하였다. 형질전환체에서 mTGase의 발현을 Northern hybridization을 통해 확인하였으며, 최대 26 mU/ml의 mTGase의 활성을 측정할 수 있었다.

Keywords

References

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