The Secretion of Streptomyces monbaraensis Transglutaminase From Lactococcus lactis and Immobilization on Porous Magnetic Nanoparticles.

ABSTRACT: Microbial transglutaminase (MTG) from Streptomyces mobaraensis is an important enzyme widely applied in food processing for the improvement of protein properties by catalyzing the cross-linking of proteins. In this work we aimed at improving the production and enabling an easy and efficient purification process from culture supernatants. Thus, recombinant vectors, with either a constitutive promoter (P _p5 ) or an inducible promoter (P _nisA ), controlling the expression of the MTG gene fused to the signal peptide of Usp45 (SP _usp45 ) were constructed and then expressed in Lactococcus lactis. After purification, 43.5 ± 0.4 mg/L mature MTG-6His was obtained. It displayed 27.6 ± 0.5 U/mg enzymatic activity cross-linking soy pr

SUBMITTER: Ma T 

PROVIDER: S-EPMC6691175 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature