Abstract: Hypertension is a considerable public health problem worldwide. Angiotensin-Ⅰ converting enzyme (dipeptidylcarboxypeptidase, EC 3.4.15.1, ACE) plays a critical role in regulating blood pressure through the renninangiotensin system (RAS) and kallikrein-kinnin system (KKS). Recently, numerous studies aimed at alleviating hypertension have focused on the generation and isolation of ACE-inhibitory peptides from various food sources. A number of studies have reported the structure-activity relationship of food protein-derived antihypertensive peptides, especially the effect of the primary structure on the potency. Compared with synthetic chemical drugs, ACE inhibitory peptides derived from food proteins are considered to be safer and milder. Nowadays, one of the most widely used techniques to liberate ACE inhibitory peptides is enzymatic hydrolysis. This technique involves one or more proteases at the optimum temperature and pH conditions. In this review, in order to provide a theoretical guidance for the preparation of high-quality ACE inhibitory peptides, we review recent reports on the structure-activity relationship and enzymatic preparation of ACE inhibitory peptides.

Key words: angiotensin-Ⅰ converting enzyme inhibitors, antihypertensive mechanism, structure-activity relationship, enzymatic preparation