Conjugation of the glutelin hydrolysates-glucosamine by transglutaminase and functional properties and antioxidant activity of the products

A novel mixture of glycopeptides was prepared from corn glutelin and glucosamine (GlcN). The functional properties and antioxidative activities of this mixture were investigated. Corn glutelin was limited hydrolyzed by Alcalase, and then its hydrolysates were glycosylated with GlcN by transglutaminase (TGase) to modify its main and side chain, respectively. Under the optimized conditions, the content of GlcN conjugated to peptides was 81.98 ± 1.98 mg/g glutelin peptides. According to electrospray ionization mass spectrometry (ESI-MS) analysis, there are two types of glycopeptides in the mixture, TGase and non-enzymatic glycated counterparts. Compared with original glutelin, the glycosylated glutelin hydrolysates exhibited better solubility in the pH range of 2-11 and other functional properties except foaming stability. Meanwhile, it is more easily digested by pepsin and trypsin, and possessed excellent antioxidative activities. It also exhibited cytoprotective effects and intracellular ROS scavenging activities in LO2 cells subjected to oxidative stress by oxidation with ethanol solution.