Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 24, Issue 15, Pages -Publisher
MDPI
DOI: 10.3390/ijms241512402
Keywords
transglutaminase; industrial enzyme; protein-modifying enzyme; crosslinker; antibody-drug conjugation; immobilization
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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.
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