Abstract

Fish protein hydrolysates have attracted much attention of food biotechnologists in recent years due to the availability of large quantities of raw materials in the fish industry waste to produce this material, and due to their high protein content with good amino acid balance and bioactive peptides (antioxidant, antihypertensive, immunomodulatory and antimicrobial peptides) (22). Some properties exhibited or expressed by bioactive peptides include antihypertensive or enzyme inhibitory properties (23) and cholesterol lowering properties (24). Biologically active roles associated with fish peptides include Angiotensin converting enzyme (ACE) inhibition (25). This article will review the roles of salmon peptides extract in the health of cardiovascular system. Online literature searches were performed to identify the studies about the benefits of salmon peptide extract.

Introduction

Hypertension represents one of the major independent risk factors for myocardial infarction, congestive heart failure, arteriosclerosis, stroke, and end-stage renal disease (29).

Angiotensin- I converting enzyme (ACE) plays an important role in the regulation of blood pressure and hypertension (30). Bioactive peptides usually contain 3–20 amino acid residues and their activities are based on their amino acid composition and sequence (15). These peptides are reported to be involved in various biological functions such as antihypertension, immunomodulatory, antithrombotic, antioxidant, anticancer and antimicrobial activities, in addition to nutrient utilization (15)(16).

This review article will highlight the findings of previous studies on the roles of salmon peptides extract against the health of cardiovascular system in mammals.

Function (Anti-hypertension, lowering cholesterol and triglycerides)

Bioactive peptides isolated from various fish protein hydrolysates have shown numerous bioactivities such as antihypertensive, antithrombotic (17)(18)(19), anticoagulant (20), immunomodulatory and antioxidative activities (20)(21). ACE-inhibitory peptides isolated and identified in gelatine hydrolysates derived from chum salmon cartilage (31).

Oral administration of protein hydrolysates derived from sea bream scales and salmon skins may successfully decrease blood pressure in spontaneously hypertensive rats (31) (33).

Other species/raw materials with protein hydrolysates with documented ACE‐inhibition are ‐ salmon and chum salmon (27)(28). Studies on fish peptides have demonstrated antihypertensive (1)(2)(3)(4).

Hydrolyzed proteins from fish have been demonstrated to alter the cholesterol and lipid metabolism in rodent studies, and to reduce plasma cholesterol and triglyceride levels (5)(6)(7) (8).

Kim, Choi, Park, Choi, and Moon (13) have reported that some peptides derived from fish showed antihypertensive activity inhibiting the action of angiotensin I converting enzyme (ACE) even stronger than that of many other natural peptides. These peptides exhibited in vivo activities by lowering blood pressure in spontaneously hypertensive rats (14).

A class of such peptides is the angiotensin inhibitory peptides; these have the effect of reducing the rate at which the vasoconstrictor, angiotensin-II is produced and regulates hypertension (26).

In addition, previous study found a reduction in hepatic ∆5 and ∆6 desaturase mRNA expression in obese Zucker rats by a fish protein hydrolysate (FPH) diet (9).

A cholesterol lowering effect of FPH diets compared to casein diets have previously been observed in rodents, and may be due to decreased intestinal absorption concomitant with increased hepatic excretion of cholesterol and bile (10) (11).
FPH has in some rodent studies also resulted in lower plasma triacylglycerol (TAG) levels (8) (12).

Conclusion

Through multiple investigations, salmon peptide extract has shown promise as an agent of anti-hypertension, lowering blood cholesterol and reducing the triglycerides level of animal models. Its consumption may benefit in the health of cardiovascular system in pet animals contributing to longevity and mutability.

References

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