Effect of gelatin on gelation properties of oyster (Crassostrea gigas) protein

The purpose of this study was to explore the effect of gelatin on the formation of oyster protein gel and reveal the interaction mechanism between gelatin and oyster protein. In the present study, the oyster protein (OP100) was obtained after being high pressure homogenized (100 MPa) and subsequently reconstituted with different concentrations (0, 2.0, 4.0, 6.0, and 8.0%) of gelatin. The rheological results showed that gelatin improved the storage modulus of OP100, and accelerated the gelation of OP100 during the cooling period. Moreover, gelatin improved the gel strength and texture properties of OP100. Infrared scanning indicated that new hydrogen bonds and β-sheets structures had been formed between the OP100 and gelatin. Molecular force results showed that hydrophobic interaction, hydrogen bonds, and disulfide bonds were the main molecular forces of the OP100/gelatin composite gel. These results provide a new reference for developing oyster protein nutritional gel products and reveal that gelatin can improve the texture properties of oyster protein gel.