Transglutaminase-catalyzed glycosylation of vegetable proteins. Effect on solubility of pea legumin and wheat gliadins

The preparation of an oligochitosan‐glycosylated and cross‐linked caseinate obtained by a microbial transglutaminase and its functional properties

“…Oligosaccharide or monosaccharide with alkylamine or amine groups could be incorporated into succinylated β‐casein (Yan and Wold ), alkylated β‐gliadins or legumin (Colas et al . ) by TGase. TGase also was able to incorporate glucosamine of 1.2 mol/mol protein (about 10 g/kg protein) into caseinate (Jiang and Zhao ).…”

Effects of Fragmentation and Deamidation on the Antioxidative Activity of C Hordein.

“…The following are suggested as methods to improve the functional characteristics of C hordein while preventing fragmentation. The first method is the introduction of primary amines (31)(32)(33)(34)(35) and acidic carbohydrates (36,37) to the glutamine residues which were targeted by TGase. The second method is phosphorylation (38).…”

Transglutaminase‐catalyzed amination of pea protein peptides using the biogenic amines histamine and tyramine

“…TGase catalyzes the acyl‐transfer between an acyl donor, like the γ ‐carboxamide group of peptide‐ or protein‐bound glutamine residues, and an acyl acceptor, including a variety of primary amines . This reaction modifies proteins either by forming intra‐ and intermolecular isopeptide bonds via ϵ ‐( γ ‐glutamyl‐lysine) links or by the covalent attachment of amines, such as polyamine or putrescine . Microbial transglutaminase (MTGase) from Streptomyces mobaraensis is a Ca 2+ ‐independent enzyme used in various food applications due to its availability, ease of handling and stability over a wide range of pHs and temperatures .…”