FitzGerald R J, Meisel H
University of Limerick, Life Science Department, Limerick, Ireland.
Nahrung. 1999 Jun;43(3):165-7. doi: 10.1002/(SICI)1521-3803(19990601)43:3<165::AID-FOOD165>3.0.CO;2-2.
Angiotensin-I-converting enzyme (ACE) has been classically associated with the renin-angiotensin system which regulates peripheral blood pressure. Peptides derived from the major whey proteins, i.e. alpha-lactalbumin (alpha-la) and beta-lactoglobulin (beta-lg) in addition to bovine serum albumin (BSA), inhibit ACE. Some of these inhibitory peptides, i.e. alpha-lactorphin (alpha-la f(50-53)), beta-lactorphin (beta-lg f(102-105)), beta-lactotensin (beta-lg f(146-149) and albutensin A (BSA f(208-216)), have other bioactivities. The most potent lactokinin reported to date, (beta-lg f(142-148)), has an ACE IC50 of 42.6 mumol/l. While they do not have the inhibitory potency of synthetic drugs commonly used in the treatment of hypertension, these naturally occurring peptides may represent nutraceutical/functional food ingredients for the prevention/treatment of high blood pressure. Studies with gastric and pancreatic proteinase digests of whey proteins indicate that enzyme specificity rather than extent of hydrolysis dictates the ACE inhibitory potency of whey hydrolysates.
血管紧张素转换酶(ACE)一直以来都与调节外周血压的肾素-血管紧张素系统密切相关。源自主要乳清蛋白的肽,即α-乳白蛋白(α-la)、β-乳球蛋白(β-lg)以及牛血清白蛋白(BSA),均可抑制ACE。其中一些抑制性肽,如α-乳激肽(α-la f(50 - 53))、β-乳激肽(β-lg f(102 - 105))、β-乳紧张素(β-lg f(146 - 149))和白蛋白紧张素A(BSA f(208 - 216)),还具有其他生物活性。迄今为止报道的最有效的乳激肽(β-lg f(142 - 148)),其ACE IC50为42.6 μmol/L。虽然它们不具备常用于治疗高血压的合成药物的抑制效力,但这些天然存在的肽可能代表用于预防/治疗高血压的营养保健品/功能性食品成分。对乳清蛋白进行胃蛋白酶和胰蛋白酶消化的研究表明,酶的特异性而非水解程度决定了乳清水解产物的ACE抑制效力。