Laboratory for Separation Processes and Product Design, Faculty of Chemistry and Chemical Engineering, University of Maribor, Smetanova Ulica 17, SI-2000 Maribor, Slovenia.
Faculty of Medicine, University of Maribor, Taborska Ulica 8, SI-2000 Maribor, Slovenia.
Int J Mol Sci. 2023 Aug 3;24(15):12402. doi: 10.3390/ijms241512402.
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.
酶转谷氨酰胺酶（TGM）的稳定性和可重复使用性是酶促过程的重要目标，因为固定化 TGM 在不同的技术和行业中起着重要的作用。TGM 可用于许多应用。在食品工业中，它作为一种蛋白质修饰酶发挥作用，而在生物技术和制药应用中，由于其非凡的交联能力，它被用于介导的生物缀合。TGM（EC 2.3.2.13）是一种酶，可催化蛋白质结合或肽结合赖氨酸的游离氨基与蛋白质结合或肽结合谷氨酰胺的γ-羧酰胺基之间形成共价键，赖氨酸作为酰基受体，谷氨酰胺作为酰基供体。这导致蛋白质通过分子内或分子间交联进行修饰，从而显著提高了各自蛋白质的用途。
