Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
