TY - JOUR
T1 - Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins
AU - Mullally, Margaret M.
AU - Meisel, Hans
AU - Fitzgerald, Richard J.
PY - 1997/5
Y1 - 1997/5
N2 - 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.
AB - 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.
KW - ACE inhibition
KW - Bioactive peptides
KW - Nutraceutical
KW - Whey protein hydrolysates
UR - http://www.scopus.com/inward/record.url?scp=0031464182&partnerID=8YFLogxK
U2 - 10.1016/S0958-6946(97)00018-6
DO - 10.1016/S0958-6946(97)00018-6
M3 - Article
AN - SCOPUS:0031464182
SN - 0958-6946
VL - 7
SP - 299
EP - 303
JO - International Dairy Journal
JF - International Dairy Journal
IS - 5
ER -