Title: Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins
Abstract: Enzymatic hydrolysates of bovine β-lactoglobulin (β-Lg), α-lactalbumin (α-La) and whey protein concentrate (WPC) were analysed for their angiotensin-I-converting enzyme (ACE) inhibitory activity. The unhydrolysed substrates gave very low ACE inhibitory indices, i.e. < 10%. Hydrolysis of the whey proteins by pepsin, trypsin, chymotrypsin and the commercially available enzyme preparations, Corolase PP and PTN 3.0S, resulted in high ACE inhibition indices, i.e. 73–90%. Hydrolysates generated with elastase displayed relatively low ACE inhibitory activity. The order of trypsin and pepsin addition during the hydrolysis of α-La and β-Lg did not appear to affect the ACE inhibitory activity of the resulting hydrolysate. Preliminary studies indicated that ultrafiltration through 3 and 1 kDa molecular mass cut-off membranes may be exploited to enrich for ACE inhibitory peptides. The ACE IC50 inhibition values obtained for ultrafiltered tryptic digests of β-Lg and WPC ranged from 130–201 mg L−1. The potential application of whey protein hydrolysates as nutraceuticals in the prevention of hypertension is discussed.
Publication Year: 1997
Publication Date: 1997-05-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 218
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