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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. [ABSTRACT FROM AUTHOR]

In recent years, there is a growing interest in the role of bioactive peptides obtained from natural food resources such as animal muscle proteins. Bioactive peptides/enzymatic protein hydrolysates are biomolecules broken down from proteins due to enzymatic hydrolysis, which usually contain 2–20 amino acids units with significant biological properties including antioxidant, anti-diabetic, and anti-cancer activities. Protein hydrolysates or peptides provide a natural therapeutics for controlling diabetes (type-II) by reducing amylase enzymatic activity and degrade the natural incretin hormone involved in blood glucose regulation. Such biological properties of peptides are highly correlated to sequence of amino acids and size. These bioactive molecules can be isolated, purified, and identified following different approaches such as gel filtration chromatography, Mass spectrometry approaches among others. In general, the animal muscles could be used as sustainable protein sources in the production of bioactive peptide-based functional foods and natural drugs for preventing chronic diseases. This review article aims to summarize the antioxidant, anti-diabetic, and anti-cancer activities of muscle proteins hydrolysates and purified bioactive peptides. [Display omitted] • This review paper discusses on functionality and bioactive characteristics of peptides. • Bioactive peptides can be produced through several enzymatic hydrolysis. • Specific bioactive peptides can be purified through different novel approaches. • Polar and non-polar peptides has anti-cancer and anti-diabetic properties. [ABSTRACT FROM AUTHOR]