Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins

Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase... 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 IC 50 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png International Dairy Journal Elsevier

Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins

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Publisher
Elsevier
Copyright
Copyright © 1997 Elsevier Ltd
ISSN
0958-6946
eISSN
1879-0143
D.O.I.
10.1016/S0958-6946(97)00018-6
Publisher site
See Article on Publisher Site

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 IC 50 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.

Journal

International Dairy JournalElsevier

Published: May 1, 1997

References

  • Whey protein fractions and their properties
    Mehra, R.

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