Whey oligopeptides were prepared from whey protein powder by enzymolysis. The basic physical and chemical composition, amino acid composition, ACE inhibitory activity and in vitro stability were investigated. The results showed that the total protein content of whey oligopeptides, acid soluble protein, water, ash and fat content were (71.83±0.37)%, (61.71±2.42)%, (4.86±0.23)%, (5.23±0.10)% and (0.21±0.05)%, respectively. Whey oligopeptides were rich in glutamic acid, leucine, aspartic acid and essential amino acids. In the range of pH 2-10, the inhibition rate of ACE changed from 48.26% to 50.91%, and the total content of peptides with the molecular weight below 1000 u fluctuated from 93.57% to 94.78%. Moreover, at 30-100 ℃, the inhibition rate of ACE fluctuated from 48.67% to 51.29%, and the total content of peptides with the molecular weight below 1 000 u fluctuated from 93.75% to 94.51%. After digestion with pepsin, trypsin, and pepsin digestion followed by trypsin digestion, respectively, the ACE inhibition rate changed from 47.63% to 50.93%, and the proportion of peptides with a molecular weight of 150-1 000 u decreased slightly. Meanwhile, the total content of peptides less than 150 u increased slightly. These results indicated that whey oligopeptides had acid-base stability, thermal stability and digestive stability under the above conditions.
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