Properties and applications of microbial transglutaminase
K Yokoyama, N Nio, Y Kikuchi - Applied microbiology and biotechnology, 2004 - Springer
Some properties and applications of the transglutaminase (TGase) referred to as microbial
TGase (MTGase), derived from a variant of Streptomyces mobaraensis (formerly classified …
TGase (MTGase), derived from a variant of Streptomyces mobaraensis (formerly classified …
Transglutaminase and its use for food processing
M Motoki, K Seguro - Trends in food science & technology, 1998 - Elsevier
Some characteristics and applications of a transglutaminase, derived from a variant of
Streptoverticillium mobaraense, namely microbial transglutaminase (MTGase), are …
Streptoverticillium mobaraense, namely microbial transglutaminase (MTGase), are …
Microbial transglutaminase and its application in the food industry. A review
M Kieliszek, A Misiewicz - Folia microbiologica, 2014 - Springer
The extremely high costs of manufacturing transglutaminase from animal origin (EC 2.3.
2.13) have prompted scientists to search for new sources of this enzyme. Interdisciplinary …
2.13) have prompted scientists to search for new sources of this enzyme. Interdisciplinary …
Recent advances in microbial transglutaminase biosynthesis and its application in the food industry
Abstract Background Microbial transglutaminase (MTGase) has been widely used to modify
the functional properties of proteins in food systems. In the last 30 years since the discovery …
the functional properties of proteins in food systems. In the last 30 years since the discovery …
Innovation in the food industry using microbial transglutaminase: Keys to success and future prospects
N Miwa - Analytical biochemistry, 2020 - Elsevier
Transglutaminase (TG) catalyzes cross-linking between the γ-carboxyamide groups of
glutamine residues and the ε-amino groups of lysine residues in polypeptide chains …
glutamine residues and the ε-amino groups of lysine residues in polypeptide chains …
Novel applications for microbial transglutaminase beyond food processing
Y Zhu, J Tramper - Trends in Biotechnology, 2008 - cell.com
Transglutaminase (EC 2.3. 2.13) initially attracted interest because of its ability to
reconstitute small pieces of meat into a 'steak'. The extremely high cost of transglutaminase …
reconstitute small pieces of meat into a 'steak'. The extremely high cost of transglutaminase …
Microbial transglutaminase—a review of its production and application in food processing
Y Zhu, A Rinzema, J Tramper, J Bol - Applied microbiology and …, 1995 - Springer
Abstract Transglutaminase (EC 2.3. 2.13) catalyses an acyl-transfer reaction in which the γ-
carboxamide groups of peptide-bound glutaminyl residues are the acyl donors. The enzyme …
carboxamide groups of peptide-bound glutaminyl residues are the acyl donors. The enzyme …
Review transglutaminases: part II—industrial applications in food, biotechnology, textiles and leather products
Because of their protein cross-linking properties, transglutaminases are widely used in
several industrial processes, including the food and pharmaceutical industries …
several industrial processes, including the food and pharmaceutical industries …
Overproduction of Microbial Transglutaminase in Escherichia coli, In Vitro Refolding, and Characterization of the Refolded Form
K YokoyAMA, N Nakamura, K Seguro… - Bioscience …, 2000 - academic.oup.com
The Streptoverticillium transglutaminase (MTG) gene, synthesized previously for yeast
expression, was modified and resynthesized for overexpession in E. coli. A high-level …
expression, was modified and resynthesized for overexpession in E. coli. A high-level …
Purification, characterisation, and gene cloning of transglutaminase from Streptoverticillium cinnamoneum CBS 683.68
R Duran, M Junqua, JM Schmitter, C Gancet, P Goulas - Biochimie, 1998 - Elsevier
The transglutaminase (TGase; EC 2.3. 2.13) from Streptoverticillium cinnamoneum CBS
683.68 has been purified, characterised and its gene cloned. The purified enzyme had a …
683.68 has been purified, characterised and its gene cloned. The purified enzyme had a …