Transglutaminase-mediated glycosylation enhances the physicochemical and functional properties of ovalbumin

This investigation mainly aimed to synthesize transglutaminase (TGase)-catalyzed glycosylated ovalbumin (TGaseOVA) and elucidate the effect of diverse enzymatic reaction durations (from 1 h to 5 h) on the physicochemical, structural, and functional properties of glycosylated ovalbumin. Following a 4 h TGase reaction, the level of graft glycosylation reached 36.6%. Electrophoretic analysis provided evidence on the presence of high-molecular-weight glycoprotein polymers in the modified product. The glucosamine (GlcN) content measured 16.6 mg/g during high-performance liquid chromatography. Furthermore, compared with the original protein, TGaseOVA exhibited a stable three-dimensional network structure. After GlcN grafting, structural changes were analyzed in terms of intermolecular and intramolecular covalent crosslinking within the protein, and the results confirm that these modifications considerably improved the functional properties of TGaseOVA particles. This study demonstrates prospects for the development of novel protein compositions to broaden applications of food proteins.