Antioxidant Activity And Amino Acid Composition Of Collagen Peptide In Sheep Bone

In this experiment,goat bone powder was used as raw material,which was pretreated and collagen was extracted by enzymatic method,and the structure of collagen was identified Papain and trypsin were used to hydrolyze collagen,collagen peptide was obtained by centrifugation and then freeze-dried.The hydrolysis degree,peptide yield,antioxidant activity and amino acid sequence were determined.The experimental results are as follows:1.The result of SDS-PAGE that the collagen extracted from sheep bone was mainly type I collagen,and the molecular weight is about 120KDa.2.Papain and the Trypsin were selected to hydrolysis Sheep bone collagen to gain the optimal processing parameter based on the degree of hydrolysis and the peptide yield.Under the optimal processing conditions,the hydrolysis degree of trypsin was 13.27%,and the peptide yield was 82.14%,among which small peptides below 1000 Da accounted for 96.4%.Peptide papain hydrolysis degree was 12.15%,the yield was 85.73%,and all the molecular weight peptides are under 1000 Da.3.Hydroxyl radical scavenging ability,superoxide anion scavenging ability and total reducing ability were identified by Vc as a control group by collagen peptides hydrolyzed by different enzymes.The results were as follows:when the concentration of peptide solution reached 1.5mg/mL,the hydroxyl radical scavenging ability of the peptide solution hydrolyzed by trypsin was significantly higher than that of the control group,,but the difference was not significant(P>0.05),and the values were 92.28%and 86.39%,respectively.When the concentration of peptide solution was 20 g/mL,the superoxide anion scavenging rate was the highest,with the values of 59.53%and 51.29%.The superoxide anion scavenging ability of the peptide solution obtained by trypsin and papain hydrolysis was not as good as that of the control group and the difference was significant(P<0.05).When the concentration of the peptide solution was 8mg/ml,the reduction capacity of the peptides hydrolyzed by trypsin was significantly greater than that of the peptides hydrolyzed by papain(P<0.05).4.The molecular weight of the peptides obtained in this experiment was less than 1000 Da,and the length of the peptides was between 7 and 30 amino acids,and the content of 20 amino acids was less than 98%.The peptides obtained by enzymatic digestion are rich in essential amino acids,and the hydrophobic amino acids Leu,Tyr,Val,Ala,Ile,Phe and Trp are more.