Abstract:Enzymatic hydrolysates EP1 and EP2 were prepared from chicken salt-soluble protein and myofibrillar protein, respectively. Their molecular weight distribution, free amino acids, and reducing power, as well as ·OH free radical, O2-·free radical and DPPH· free radical scavenging powers were analyzed. The results showed that the molecular weights of EP1 and EP2 were below 5000 u, and their constituents with a molecular weight range of 180~1000 u accounted for 66.32% and 54.74%, while oligopeptides accounted for 57.79% and 47.70%, respectively. The analysis of free amino acids revealed that EP1 and EP2 contained many unconventional amino acids such as gamma-aminobutyric acid, taurine, carnosine and phosphoserine, besides 20 kinds of conventional amino acids. In addition, the contents of basic amino acids (26.01% and 29.43%) and hydrophobic amino acids (38.00% and 32.88%) were relatively high. EP1 and EP2 both had strong total reducing power, and ·OH radical, O2-·radical and DPPH· radical scavenging powers, that is, the ability of acting as both electron donor and hydrogen donor to scavenge free radicals. The high antioxidant activity of EP1 and EP2 resulted from the interaction of oligopeptides and amino acids.