Preparation And Identification Of Antioxidant And Hypoglycemic Bioactive Peptide From Camel Blood

Animal blood is the main by-product of the slaughtering process of livestock and poultry.It is rich in protein and other nutrients.Because the camel lives in harsh and hard environment,the special environment makes the blood more special physiological and nutritional functions than the blood of other animals.However,the utilization of camel blood is extremely low,causing great waste.In this study,the camel blood peptide is prepared by enzymatic hydrolysis to explore the antioxidant and hypoglycemic activities of the enzymatic products of different proteases.On the basis of this,the anti-oxidation and hypoglycemic peptides are separated and purified by ultrafiltration and chromatography.Finally,the amino acid composition,molecular weight distribution and amino acid sequence of the isolated and purified anti-oxidation and hypoglycemic peptides are determined.The main research results are as follows:(1)Pepsin at the optimum pH and temperature conditions,the enzymatic hydrolysis time is 3 h,the enzyme concentration is 5 mg/100mg,and the ratio of material to liquid is 1:10,the enzymatic hydrolysate has the highest antioxidant activity;By separation and purification,the component Pep-1 had the strongest antioxidant activity,and its DPPH·clearance rate was 72.6%,iron ion chelation ability was 94.9%,and total antioxidant capacity(ABTS method)was 1.433 mmol/g.The amino acid composition of the component Pep-1 was determined by automatic amino acid analyzer and found to have an amino acid content of 73.763 mg/100mg.The molecular weight and amino acid sequence of the component Pep-1 were determined by MALDI-TOF-TOF.It was mainly composed of a peptide with a molecular weight of 5107 Da.Further hydrolysis of the peptide revealed that it was mainly composed of a nonapeptide with a molecular weight of 1223.6233 Da.The amino acid sequence is Val-Val-Tyr-Pro-Trp-Thr-Arg-Arg-Phe,and most of it consists of hydrophobic amino acids.(2)At the optimum pH and temperature,the enzymatic hydrolysis time was 4 h,the enzyme concentration was 5 mg/100mg,and the ratio of material to liquid was 1:6.The enzymatic hydrolysate had the highest ?-amylase inhibitory activity and A-glucosidase inhibitory activity.By separation and purification of the a-amylase inhibition rate of the component Fla-a(66.03%)was the highest,and the a-glucosidase inhibition rate of Fla-b was the highest(90.86%).The amino acid composition of the components Fla-a and Fla-b was determined by a fully automatic amino acid analyzer.The content of Fla-a amino acid was 81.630 mg/100mg,and the amino acid content of component Fla-b was 49.126 mg/100mg.The molecular weight and amino acid sequence of the components Fla-a and Fla-b were determined by MALDI-TOF-TOF.It was found that the component Fla-a was mainly composed of a hexapeptide with a molecular weight of 722.3637 Da and the amino acid sequence was Tyr-Pro-Gly-Glu-Thr-Arg;component Fla-b is mainly composed of a hexapeptide having a molecular weight of 878.4473 Da,and the amino acid sequence is Tyr-Pro-Trp-Thr-Arg-Arg.Conclusion:In this study,we isolated and purified the camel blood antioxidant peptide Val-Val-Tyr-Pro-Trp-Thr-Arg-Arg-Phe with a molecular weight of 1223.6233 Da and the hypoglycemic peptide Tyr-Pro-Gly-Glu-Thr-Arg,Tyr-Pro-Trp-Thr-Arg-Arg with a molecular weight of 722.3637 Da and 878.4473 Da,respectively.