Transglutaminase in Foods and Biotechnology.
antibody–drug conjugation
crosslinker
immobilization
industrial enzyme
protein-modifying enzyme
transglutaminase
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
03 Aug 2023
03 Aug 2023
Historique:
received:
26
07
2023
revised:
01
08
2023
accepted:
02
08
2023
medline:
14
8
2023
pubmed:
12
8
2023
entrez:
12
8
2023
Statut:
epublish
Résumé
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 γ-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.
Identifiants
pubmed: 37569776
pii: ijms241512402
doi: 10.3390/ijms241512402
pmc: PMC10419021
pii:
doi:
Substances chimiques
Transglutaminases
EC 2.3.2.13
Proteins
0
Peptides
0
Glutamine
0RH81L854J
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Slovenian Research Agency
ID : P2-0046
Organisme : Slovenian Research Agency
ID : J2-3037
Organisme : Slovenian Research Agency
ID : Z2-4431
Organisme : Slovenian Research Agency
ID : L2-4430
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