Study On Preparation Of Angiotensin Converting Enzyme Inhibitory Peptide And Antioxidant Protein Peptide From Chickpea

Active Peptides are special protein fragments which play an important part in thefunction and station of organism and affect our health. In order to exert the function ofantioxidation it reduces oxygen free radicals and hydroxyl radicals. Chickpea separationprotein was enzymed by alkaline protease to produce ACE inhibitory peptide, the effect oftemperature, pH, time, and enzyme substrate ratio was explored to optimize the hydrolysisconditions of chickpea separation protein through Box-Benhnken response surface analysison the basis of single-factor experiments, valued by ACE inhibition.The optimal hydrolysistemperature, pH, time, and enzyme substrate ratio were indicated to be50℃,8.0,4%and4.0h.Under these conditions the predicted percentage was,which was consistent with theaverage of replicates of (59.01±0.58)%obtained in the validation experiments.In this article we use ether to defat the chickpea flour, and use Isoelectric point methodextract chickpea protein, use alkaline protein enzyme on chickpea protein to get chickpeapeptide, use folin to evaluate peptide content, use DPPH methods, FRAP method,ABTSmethod and FERROZINE method to test the antioxidant activity in vitro of chickpeapeptide.The results showed that the chickpea protein peptide content of hydrolysis is349.6g/L. The clearance rate of chickpea peptide to DPPH free radical was20.31μmol/L, with theIC5083.49g/L. The clearance rate of chickpea peptide to ABTS free radical was117.33μmol/L. The TEAC showed15.34μmol/L in FRAP methods, with IC5037.4g/L.While the concentration of sample reaches50g/L, concentration of EDTA reaches0.042g/L,the IC50reaches55.52g/L.From the four methods about chickpea protein peptide antioxidantactivity we can get that between specific concentration regions and antioxidant activity ofpeptides has a good correlation in different methods. All of the above showed that chickpeaspeptides had strong antioxidant activity.