Korean Journal of Mycology (Kor. J. Mycol.)
Hyoun-Young Kim 1*, Dong-Soon Oh 2 and Jong-Hwa Kim 2
1Institute of Basic and Natural Science, Woosuk University,
2Department of Pharmaceutical Engineering, Woosuk University
Correspondence to kangwon@woosuk.ac.kr
Korean Journal of Mycology (Kor J Mycol) June 30, 2008, 36(1):93-97.
https://doi.org/10.4489/kjm.2008.36.1.093
(Received May 26, 2008. Accepted June 25, 2008)
Published: June 30, 2008.
© The Korean Society of Mycology
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.
Heterologus gene expression, Kluyveromyces marxianus, Microbial transglutaminase, Saccharomyces cerevisiae, Streptomyces mobaraensis