Abstract

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

Details

Title
Production of transglutaminase in glutathione-producing recombinant Saccharomyces cerevisiae
Author
Hirono-Hara Yoko 1 ; Miyuu, Yui 1 ; Hara, Kiyotaka Y 2   VIAFID ORCID Logo 

 University of Shizuoka, Department of Environmental and Life Sciences, School of Food and Nutritional Sciences, Shizuoka, Japan (GRID:grid.469280.1) (ISNI:0000 0000 9209 9298) 
 University of Shizuoka, Department of Environmental and Life Sciences, School of Food and Nutritional Sciences, Shizuoka, Japan (GRID:grid.469280.1) (ISNI:0000 0000 9209 9298); University of Shizuoka, Graduate Division of Nutritional and Environmental Sciences, Shizuoka, Japan (GRID:grid.469280.1) (ISNI:0000 0000 9209 9298) 
Publication year
2021
Publication date
Jan 2021
Publisher
Springer Nature B.V.
e-ISSN
21910855
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2476049442
Copyright
© The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.