Advancement and prospects of production, transport, functional activity and structure-activity relationship of food-derived angiotensin converting enzyme (ACE) inhibitory peptides. Issue 10 (15th April 2023)

• Record Type: Journal Article
• Authors: Xiang, Lu; Qiu, Zhichang; Zhao, Renjie; Zheng, Zhenjia; Qiao, Xuguang
• Is Part Of: Critical reviews in food science and nutrition. Volume 63:Issue 10(2023)
• Page Start: 1437
• Page End: 1463
• Publication Date: 2023-04-15
• Subjects: Antihypertensive peptides -- food origins -- preparation -- transport -- underlying mechanism -- structure-activity relationship; Food industry and trade -- Periodicals; Nutrition -- Periodicals; Nutrition -- Periodicals; Food -- Periodicals; Diet -- Periodicals; Review Literature -- Periodicals; Nutrition; Food; Diet; Review Literature; 664
• DOI: 10.1080/10408398.2021.1964433
• Languages: English
• ISSNs: 1040-8398

Abstract

Abstract: Food-derived antihypertensive peptides have attracted increasing attention in functional foods for health promotion, due to their high biological activity, low toxicity and easy metabolism in the human body. Angiotensin converting enzyme (ACE) is a key enzyme that causes the increase in blood pressure in mammals. However, few reviews have summarized the current understanding of ACE inhibitory peptides and their knowledge gaps. This paper focuses on the food origins and production methods of ACE inhibitory peptides. Compared with conventional methods, the advanced technologies and emerging bioinformatics approaches have recently been applied for efficient and targeted release of ACE inhibitory peptides from food proteins. Furthermore, the transport and underlying mechanisms of ACE inhibitory peptides are emphatically described. Molecular modeling and the Michaelis-Menten equation can provide information on how ACE inhibitors function. Finally, we discuss the structure-activity relationships and other bio-functional properties of ACE inhibitory peptides. Molecular weight, hydrophobic amino acid residues, charge, amino acid composition and sequence (especially at the C-terminal and N-terminal) have a significant influence on ACE inhibitory activity. Some studies are required to increase productivity, improve bioavailability of peptides, evaluate their bio-accessibility and efficiency on reducing blood pressure to provide a reference for the development and application of health products and auxiliary treatment drugs.