Molecular Cloning and Overexpression of the Transglutaminase Gene from <i>Streptomyces mobaraensis</i>

Tissue transglutaminase Cloning (programming) Strain (injury) Target protein
DOI: 10.3136/fstr.25.687 Publication Date: 2019-10-23T22:04:06Z
ABSTRACT
Transglutaminase-catalyzed reactions can be used widely to modify the functional properties of food proteins, biopharmaceuticals and in tissue engineering. Streptomyces mobaraensis is important for industrial fermentation because its rapid, low-cost growth easy cultivation. We cloned transglutaminase (TGase) gene from S. mobaraensis; was 1224-bp (65.22% G+C), encoding 407 amino acids. Then, expression vector pL99-T constructed by cloning TGase into plasmid pL99. introduced using conjugation protoplast transformation method, respectively. observed activity 8.68 U/mL transformant SMP-12, 5.88-fold that original strain (1.26 U/mL); moreover, protein higher than strain. These results suggest directed overexpression effectively enhance production mobaraensis. This method enhanced active may valuable applications.
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