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Vol 3:3 Properties of Proteins Relate to Their Contribution to the 168 Physiochemicalf and Sensory Properties of Foods

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Vol 3:3 Properties of Proteins Relate to Their Contribution to the 168 Physiochemicalf and Sensory Properties of Foods Popular Article Journal Home: www.bioticainternational.com Article: RT520 How to cite this article? Biotica Vinoth et al., 2021. Food Derived Peptides – Role in Research [Human Health. Biotica Research Today 3(3): 165-168. [ Today Abstract ood proteins have long been recognized for their nutritional 165 and functional properties. On the other hand, the functional Vol 3:3 properties of proteins relate to their contribution to the 168 physiochemicalF and sensory properties of foods. Nowadays, a 2021 considerable amount of research has also focused on bioactive peptides which are present in foods, and researchers are trying Food Derived Peptides – to utilize such peptides as functional food ingredients aimed at health maintenance. Several bioactive peptides such as antioxidant, Role in Human Health antihypertensive, antiproliferative, antimicrobial, neuroactive, * hormonal and mineral binding were isolated from the fishes Vinoth Kumar L. , Manivannan M. and and shellfishes. The process flow of bioactive peptides includes Vignaesh D. purification and filtration methods and the peptide sequence was identified. The commercial application were also reported and Paraprofessional Institute of Fisheries Technology, Tamil Nadu discussed by many researches. Although the efficacies of these Dr. J. Jayalalithaa Fisheries University, Madhavaram, Chennai, peptides were wide range, the safety and conditions of usage are Tamil Nadu (600 051), India yet to be proven. Introduction t has been defined as specific protein fragments that have a Open Access positive impact on body functions and conditions and may Corresponding Author Iultimately influence health. Bioactive peptides have been defined as peptides with hormone- or drug like activity that Vinoth Kumar L. e-mail: [email protected] eventually modulate physiological function through binding interactions to specific receptors on target cells leading to induction of physiological responses (Murray and Fitzgerald, 2007). These are proteins synthesized in the cell in the form of Keywords large pre pro peptides, which are then cleaved and modified ACE inhibitory peptides, Bioactive properties, Peptides, to give active products. Interestingly, within the protein Protein hydrolysates sequence, the peptides are inactive and thus must be released to exert an effect. Usually bioactive peptides are 2–20 amino acid residues in length, although, some have been reported to be more than 20. History of Bioactive Peptide Discovery he first food-derived bioactive peptide was identified in casein phosphorylated peptides enhanced vitamin TD-independent bone calcification in rachitic infants (Mellander, 1950). However, interest in this field has increased considerably in the last two decades, with the majority of research focusing on the identification of bioactive peptides from milk proteins. Article History Classification Received in 11th March 2021 Received in revised form 17th March 2021 ased on the functional properties, bioactive peptides are Accepted in final form 18th March 2021 Bclassified in to several types. E-mail: [email protected] © 2021 165 Vinoth et al., 2021 between the associated vasoconstrictive and salt-retentive attributes of Ang ІІ with the vasodilatory effect of bradykinin. The balance is maintained by decreasing the production of Ang ІІ and reducing the degradation of bradykinin. While synthetic ACE inhibitors, such as Captopril function by directly blocking the action of ACE, ACE inhibitory peptides function by reacting with ACE, thus ACE is unavailable to cleave AngІ and prevent the production of the vasoconstrictor Ang ІІ. In the past decade, it has been reported that muscle proteins from animals are a viable source of ACE inhibitory peptides in vitro and may potentially be incorporated into nutraceutical products to exert antihypertensive effects in vivo. Figure 1: Graphical representation of different types of bioactive peptides Antihypertensive Peptides ntihypertensive peptides may contribute to the lowering of blood pressure through inhibition of enzymes including ACE or endothelin converting A Figure 2: Mechanism of action of ACE inhibitory peptides enzyme (ECE). ACE inhibitory peptides were first discovered in snake venom and since then numerous synthetic ACE inhibitors have been produced, with Captopril being the most Antioxidative Peptides common. Captopril and other synthetic ACE inhibitors are ntioxidants are known to be beneficial to human known to exert various side-effects such as coughing, taste health as they may protect the body against molecules disturbances and skin rashes. These side effects, coupled with known as reactive oxygen species (ROS), which can the fact that hypertension affects one third of the Western A attack membrane lipids, protein and DNA. This in turn can worlds’ population and is a known risk factor for stroke and be a causative factor in many diseases such as cardiovascular cardiovascular disease, has contributed to the ongoing search disease, diabetes cancer and Alzheimer’s disease. Lipid for food derived antihypertensive peptides for exploitation as oxidation can cause deterioration of food quality and a antihypertensive agents in functional foods and nutraceuticals. reduction in the shelf-life of a food product, while the Mechanism of ACE Inhibition consumption of foods containing lipid oxidation products has been linked to various diseases, including cancers, diabetes n the rennin-angiotensin system, Angiotensinogen present and cardiovascular disease. in the liver has been converted into angiotensin I, by The use of natural antioxidants in foodstuffs is appealing the action of renin which is released from kidney. ACE because of the potential health risk associated with synthetic Icatalyses the conversion of the inactive form of angiotensin antioxidants in vivo. Antioxidant peptides have been found I (Ang І) to the potent vasoconstrictor angiotensin II (Ang in numerous foodstuffs including milk, wheat, potato and ІІ). Additionally, ACE is involved in the deactivation of the fungi. In the past number of years, a great deal of research hypotensive peptide, bradykinin. This is as a result of ACE has focused on antioxidant peptides sourced from fish, while cleaving the C-terminal dipeptide from Ang І (His-Leu) and bradykinin. Ang ІІ is a documented potent vasoconstrictor the research on antioxidant peptides from the hydrolysates of which acts directly on vascular smooth muscle cells. Ang ІІ domesticated animal muscle is limited. There are a number of is also responsible for the expansion of vascular volume via methods available to measure antioxidant potential of various sodium retention and fluid retention. Bradykinin is responsible food components based on the ability of potential antioxidants for uterine and ileal smooth muscle contraction, enhanced to scavenge ROS, free radicals or prevent oxidation in model vascular permeability, activation of peripheral and C fibers systems. and increases in mucous secretion. Furthermore, bradykinin Antimicrobial Peptides contributes to vasodilation by advancing the assembly of arachidonic acid metabolites, nitric oxide, and endothelium- ntimicrobial peptides (AMPs) have been identified in derived hyperpolarizing factor in the vascular endothelium. a range of foods to date, with peptides released from Therefore, ACE inhibitors function by maintaining the balance Amilk proteins being the most plentiful source of AMPs. © 2021 166 Biotica Research Today 2021, 3(3):165-168 Indeed, AMPs have been found in a host of different milk of important metabolic, growth and development processes. proteins including the caseins and lactoferrin. While AMPs These peptides purified from cod hydrolysate from heads, from the protein of muscle foods are less well documented, stomach, and viscera, shrimp head hydrolysate, cooked there has been one report of AMPs from a bovine meat source. sardine head, and gut hydrolysate, and from a cooked siki In this study, the antimicrobial and human cancer cell cytotoxic (Centroscymnus coelolepsis) head hydrolysate. effects of four previously identified ACE inhibitory peptides, were evaluated. The four peptides GFHI, DFHING, FHG and Antithromotic Peptides GLSDGEWQ were assayed for antimicrobial activity against eptides isolated from anchovy sauce were capable six pathogenic bacteria, three Gram-positive (Bacillus cereus, of inducing apoptosis in a human lymphoma cell Listeria monocytogenes and Staphylococcus aureus) and line. The peptide of interest was characterized as three Gram-negative (Salmonella typhimurium, Escherichia P being hydrophobic and having a molecular weight of 440.9 coli and Pseudomonas aeruginosa). The peptide GLSDGEWQ Da. Protein hydrolysates from different fish species were inhibited the growth of S. typhimurium, B. cereus, E. coli and investigated for their antiproliferative activity on two human L. monocytogenes. This was the only peptide that inhibited the breast cancer cell lines. Hydrolysates of blue whiting, cod, growth of both Gram-positive and Gram-negative pathogens. plaice and salmon resulted in the significant inhibition of GFHI and FHG inhibited the growth of the pathogen P. growth. Recently, the hydrolysate of tuna dark muscle by- aeruginosa. product was examined for potential antiproliferative activity Neuroactive Peptides by exposure to the human breast cancer cell line. Peptide fractions within the molecular weight range of 400 and 1400 euroactive peptides exist in dairy products which play Da exhibited the strongest antiproliferative
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