ABSTRACT
Proteins are one of the primary components of food, both in terms of nutrition and function. Primary structures of many proteins comprise special regions which, on hydrolysis encrypt into some specific biofunctional peptides. Being a cheap and Nature-friendly process, hydrolysis using microbial fermentation has always been encouraged for the genesis of bioactive peptides, which can modulate the characteristics and physiological functions of in-vitro (food) and in-vivo (human) systems, respectively. However, some proteins need to be sequentially hydrolysed in both ways using microbial and extracted enzymes, for the liberation of such peptides. These food-derived peptides exhibit antihypertensive, mineral binding, antioxidative, immunomodulatory, opioid and cytomodulatory activities and are currently under investigation as new drugs for human health. Antihypertensive peptides have the ability to modulate the renin-angiotensin system (RAS) by inhibiting the activities of angiotensin-converting enzyme (ACE), the main enzyme that regulates blood pressure. Antihypertensive peptides, before exerting their pharmacokinetic effect, need to be first reached to their target sites by passing through gastrointestinal/ mucosal barriers without losing their functionality. Although, synthetic antihypertensive drugs have proved to be quite effective, safety issues of the compounds associated with them are questioned due to their unnatural molecular structures. Hence, the importance of natural antihypertensive compounds, such as peptides, has considerably increased in recent years. Therefore, this chapter focuses on antihypertensive peptides related to fermented food products, their current status, sources, production and identification. We also discuss the bioavailability of peptides during digestion and absorption of foods as well as other future perspectives.
