Calcium transglutaminase-catalyzed

A calcium-dependent transglutaminase existing in the inner root sheath and the medullary cells [186-188] catalyzed the formation of isopeptide bonds. Evidence obtained by Rogers et al. [189] suggests that proteins containing the gJu-lys bond, or, more correctly. 

Transglutaminases are acyl transfer enzymes that catalyzed the condensation of glutamine and lysine residues of proteins (51). They have been utilized for food processing. In this book a calcium-independent microbial transglutaminase has been used by Payne et al (11) to crosslink the protein in gelatin-chitosan blends... 

The enzymes used to create ELP hydrogels in a biocompatible process is transglutaminase (tTG] (Bozzini etal., 2011]. The enzyme catalyzes the calcium-dependent acyl transfer reaction that results in the formation of a y-glutamyl- -lysyl covalent bond between peptide-bound glutamine residues and various primary amines. 

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