Milk whey and casein proteins were fermented with different lactic acid starters and digestive enzymes. ACE-inhibition activity was observed only after the digestion of proteins with pepsin and trypsin. Whey proteins resulted in 35–61% inhibition and caseins 86% inhibition under the applied conditions. The hydrolysates having inhibitory activity were fractionated by size exclusion and reversed phase chromatography. Several ACE-inhibitory peptides were purified and identified by amino acid and MS-analysis. The identified peptides were α -la f105–110, β -lg f9–14, f15–20, α s1 -cn f142–147, f157–164, f194–199 and β -cn f108–113, f177–183 and 193–198. Among whey hydrolysates peptides with small molecular weight (<1000 Da) were the most active inhibitors. The highest ACE-inhibitory activity was found in the peptides derived from α s1 -casein.
International Dairy Journal – Elsevier
Published: Apr 1, 1998
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