Oxidation Inhibition and Gel Properties Enhancement of Myofibrillar Protein from Silver Carp by Bovine-bone Collagen Hydrolysate

The double enzyme digestion of bovine femur was used to obtain high quality hydrolyzed collagen from bovine bone to study the effect of bovine-bone collagen hydrolysate on oxidation and gel properties of myofibrillar protein from silver carp. The texture characteristics, structure changes and free radical scavenging ability of myofibrillar protein added with collagen hydrolysate were determined. The results showed that 1% bovine collagen hydrolysate inhibited myofibrillar protein oxidation and enhanced gel capability. Bone hydrolysate decreased the decline of total sulfhydryl groups and surface hydrophobicity and maintained dense microstructure of gel, and the highest gel strength and water retention (P<0.05) were 153.24 and 89.25% respectively. The 1% bovine collagen hydrolysate-myofibrillar protein complex had the highest scavenging ability of DPPH free radicals and hydroxyl free radicals with scavenging rates of 83.99% and 48.35%, respectively. Bovine-bone collagen hydrolysate could be used as a natural antioxidant and gel texture enhancer in freshwater fish products, and this study provided a theoretical basis for improving the quality of aquatic products.