Hernández-Ledesma Blanca, Amigo Lourdes, Ramos Mercedes, Recio Isidra
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, Spain.
J Agric Food Chem. 2004 Mar 24;52(6):1504-10. doi: 10.1021/jf034997b.
The angiotensin converting enzyme (ACE)-inhibitory activity of several commercial fermented milks was evaluated. Most of these products showed moderate inhibitory activity, but a few exceptions were detected. The high ACE-inhibitory activity found in some cases could be related to the origin of the milk. Two of these products were subjected to an enzymatic hydrolysis process, which simulates physiological digestion, to study the influence of digestion on ACE-inhibitory activity. The activity did not significantly change or increase during simulated gastrointestinal digestion. The peptides generated from one selected product during simulated digestion were sequenced by tandem spectrometry. Most peptides found at the end of the simulated digestion were released after 30 min of incubation with the pancreatic extract. This suggests that physiological digestion promotes the formation of active peptides from the proteins present in these fermented products. The potential ACE-inhibitory activity of the identified peptides is discussed with regard to their amino acid sequences.
对几种市售发酵乳的血管紧张素转换酶（ACE）抑制活性进行了评估。这些产品大多表现出中等抑制活性，但也发现了一些例外情况。在某些情况下发现的高ACE抑制活性可能与牛奶的来源有关。其中两种产品经过酶水解过程，该过程模拟生理消化，以研究消化对ACE抑制活性的影响。在模拟胃肠消化过程中，活性没有显著变化或增加。通过串联光谱法对一种选定产品在模拟消化过程中产生的肽进行了测序。在模拟消化结束时发现的大多数肽在与胰提取物孵育30分钟后释放。这表明生理消化促进了这些发酵产品中蛋白质活性肽的形成。根据已鉴定肽的氨基酸序列讨论了其潜在的ACE抑制活性。
