Purification and the secondary structure of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the al
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REVIEW ARTICLE
Purification and the secondary structure of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the alcalase hydrolysate of seahorse protein Jie Shi1 • Rui-qi Su1 • Wen-ting Zhang1 • Jian Chen1,2
Revised: 18 March 2020 / Accepted: 7 April 2020 Ó Association of Food Scientists & Technologists (India) 2020
Abstract Bioactive peptides with blood pressure-lowering functions have received increasing attention. In recent years, many ACE-inhibiting peptides have been widely purified from various food-derived proteins and have received considerable interest owing to their potential role in cardiovascular diseases and in the reduction of side effects. In this study, we hydrolyzed a three-spot seahorse (Hippocampus trimaculatus Leach) protein by alcalase to obtain a hydrolysate containing angiotensin I-converting enzyme (ACE) inhibitory peptide. Then, the hydrolysate was fractionated by dialysis, Sephadex G-25 gel filtration chromatography, and reverse-phase high performance liquid chromatography. After consecutive purification, a potent ACE-inhibiting peptide composed of 8 amino acids (Pro-Ala-Gly-Pro-Arg-Gly-Pro-Ala; MW: 721.39 Da; IC50 value: 7.90 lM) was successfully isolated from three-spot seahorse protein. For the first time, a novel ACE-inhibiting peptide (PAGPRGPA) was isolated from the seahorse. Circular dichroism (CD) analyses suggested that the secondary structure of the purified peptide was mainly composed of random coil. Therefore, the peptide from seahorse protein may be used as a favorable ingredient in nutraceuticals, medicines, and functional foods against antihypertensive and related diseases.
& Jian Chen [email protected] 1
Department of Food Science and Technology, Hainan University, No. 58, Renmin Avenue, Meilan District, Haikou 570228, China
2
State Key Laboratory of Marine Resource Utilization in South China Sea (Hainan University), Haikou 570228, China
Keywords Three-spot seahorse protein hydrolysate ACE inhibitory peptide Alcalase Protein secondary structure
Introduction In recent years, hypertension has been a serious chronic disease that can cause high-risk diseases, such as arteriosclerosis, stroke, and myocardial congestion. Hypertensive patients also show a trend of younger age (Balti et al. 2015). Hence, development of an effective treatment for hypertension is urgently needed. Angiotensin-converting enzyme (ACE, EC 3.4.15.1) is a zinc metal peptidase that regulates blood pressure via the renin–angiotensin system and the kallikrein kinin system (Ko et al. 2012). Based on the principle of ACE action, several synthetic ACE inhibitors have been developed, including captopril, lisinopril, enalapril, and alacepril. They exert significant effects on the treatment of hypertension but are also accompanied by obvious drug-associated side effects, such as cough, taste disorder, rash, and angioedema (Ahn et al. 2012). Therefore, development of non-toxic, economical, safe, and effective ACE inhibitors is important. Bioactive peptides refer to specific
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