Antihypertensive activity of fish protein hydrolysates and its peptides

Abstract

The rising interest to utilize nutritionally exorbitant fish proteins has instigated research activities in fish waste utilization. The development of newer technologies to utilize fish waste has fostered use of bioactive value-added products for specific health benefits. Enzymatically obtained Fish Protein Hydrolysate (FPH) is a rich source of biologically active peptides possessing anti-oxidant, anticancer, antimicrobial and anti-hypertensive activity. Isolating natural remedies to combat alarming negative consequences of synthetic drugs has been the new trend in current research promoting identification of antihypertensive peptides from FPH. In this review, we aim to culminate data available to produce antihypertensive peptides from FPH, its composition and potential to be used as a therapeutic agent. These purified peptides are known to be rich in arginine, valine and leucine. Reports reveal peptides with low molecular weight (<1 kDa) and shorter chain length (<20 amino acids) exhibited higher antihypertensive activity. As these peptides have proven Angiotensin Converting Enzyme - I inhibitory activity in vitro and in vivo, their potential to be used as antihypertensive drugs is outrageous. However, current focus on research in the field of molecular docking is necessary to have improved understanding of interaction of the peptides with the enzyme.

Keywords: Angiotensin converting enzyme; Fish protein hydrolysate; antihypertensive peptides; fish; proteolytic enzyme.