Abstract: Streptomyces mobaraensis transglutaminase (TGase)-activating metalloprotease (TAMEP) can specifically cleave the zymogen region of TGase to form the active form. In this study,TAMEP from S. mobaraensis was successfully expressed in Escherichia coli. Through the optimizations of signal peptide type,N-terminal codon of the signal peptide,and induction conditions,the extracellular activity of TAMEP reached 186.3 U/mL. As indicated by enzymatic analysis,that the optimal reaction temperature and pH of the recombinant TAMEP were 55 ℃ and pH 7.0,respectively. 50% activity of TAMEP was retained after incubating at 30-50 ℃ for 60 min,and the enzyme was also stable at pH 6.2-8.9. 0.133 μmol/L recombinant TAMEP can basically activated 6.91 μmol/L TGase in 30 minutes. The research results provided strains and basic data for the large-scale preparation of TAMEP.
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