4.7 Review

Transglutaminase in Foods and Biotechnology

Journal

Publisher

MDPI
DOI: 10.3390/ijms241512402

Keywords

transglutaminase; industrial enzyme; protein-modifying enzyme; crosslinker; antibody-drug conjugation; immobilization

Ask authors/readers for more resources

Stabilization and reusability of enzyme transglutaminase (TGM) are important for various technologies and industries. TGM is used in the food industry as a protein-modifying enzyme and in biotechnology and pharmaceutical applications due to its crosslinking ability. TGMs (EC 2.3.2.13) catalyze the formation of covalent bonds between protein-bound lysine and glutamine, resulting in protein modification through intramolecular or intermolecular crosslinking, enhancing their use.
Stabilization and reusability of enzyme transglutaminase (TGM) are important goals for the enzymatic process since immobilizing TGM plays an important role in different technologies and industries. TGM can be used in many applications. In the food industry, it plays a role as a protein-modifying enzyme, while, in biotechnology and pharmaceutical applications, it is used in mediated bioconjugation due to its extraordinary crosslinking ability. TGMs (EC 2.3.2.13) are enzymes that catalyze the formation of a covalent bond between a free amino group of protein-bound or peptide-bound lysine, which acts as an acyl acceptor, and the & gamma;-carboxamide group of protein-bound or peptide-bound glutamine, which acts as an acyl donor. This results in the modification of proteins through either intramolecular or intermolecular crosslinking, which improves the use of the respective proteins significantly.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available