No abstract

Nine kinds of oligopeptide were obtained from the yak bone-marrow protein via the hydrolysis of some single or mixed proteases, and the functions of various yak bone peptides were compared. The results indicated that the peptide from yak bone hydrolyzed by Alcalase plus Flavourzyme at 50 • C for 4 h showed the strongest antioxidant activity in a H 2 O 2 system and chelating activity to Cu 2+ ; Yak bone peptide derived from the hydrolysis by papain PSM500 plus Peptidase R presented the most efficient radical-scavenging activity to 2,2-diphenyl-1-picrylhydrazyl free radicals; Yak bone peptide hydrolyzed by Protamex single had the best calcium binding activity and the peptide from the hydrolysis of yak bone by trypsin displayed the most ideal chelating activity on iron (II). Taken together, yak bone peptide hydrolyzed by Alcalase plus Flavourzyme at 50 • C for 4 h had the best integration function. Therefore, it might be useful for the application in functional foods.