Production of transglutaminase in glutathione-producing recombinant Saccharomyces cerevisiae

摘要

Transglutaminase (TG) catalyzes the formation of cross-links between proteins. TG from Streptoverticillium mobaraense ( Sm TG) is used widely in food, cosmetic, biomaterial and medical industries. Sm TG is occasionally supplied as a mixture with the activator peptide glutathione. Currently, glutathione is industrially produced using a budding yeast, Saccharomyces cerevisiae , because of its intracellular high content of glutathione. In this study, active Sm TG was produced together with glutathione in S. cerevisiae . Sm TG extracted from S. cerevisiae expressing Sm TG showed cross-linking activity when BSA and sodium caseinate were substrates. The cross-linking activity of Sm TG increased proportionally as the concentration of added glutathione increased. Furthermore, Sm TG was prepared by extracting Sm TG from an engineered S. cerevisiae whose glutathione synthetic pathway was enhanced. The Sm TG solution showed higher activity when compared with a Sm TG solution prepared from a S. cerevisiae strain without enhanced glutathione production. This result indicates that a high content of intracellular glutathione further enhances active Sm TG production in S. cerevisiae . S. cerevisiae co-producing Sm TG and a higher content of glutathione has the potential to supply a ready-to-use industrial active TG solution.