Expression and Cloning of Microbial Transglutaminase in S. cerevisiae
2008
Kim, H.Y. (Woosuk University, Wanju, Republic of Korea), E-mail: [email protected] | Oh, D.S. (Woosuk University, Wanju, Republic of Korea) | Kim, J.H. (Woosuk University, Wanju, Republic of Korea)
A Ca²+-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.
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