Food Proteins and Peptides: Chemistry, Functionality, Interactions, and Commercialization
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Proteins from plant and animal origins are potential sources of a wide range of BP encrypted in their structure Carrasco-Castilla et al. Although the correlation between structure and functional properties is not well established, many BP share some structural features that include a peptide residue length between 2—20 amino acids Moller et al.
BP have also shown to be resistant to the action of digestion peptidases Kitts and Weiler, BP have been considered the new generation of biologically active regulators that can prevent, for example, oxidation and microbial degradation in foods. They can be used for the treatment of various medical conditions, thus increasing the quality of life Lemes et al. Recently, functional foods Haque et al. Consequently, considerable interest has been devoted to the production and properties of BP the past few years Przybylski et al. Even though BP have been identified and isolated from several natural sources, and their activities investigated in many disciplines, the present review is mainly concerned with BP in the context of different food matrices.
Among the macronutrients present in foods, peptides and proteins are of paramount importance, because they supply the required raw materials for protein biosynthesis and represent a source of energy Walther and Sieber, ; Dziuba and Dziuba, Also, they are part of an intricate series of organic transformations that occur during the processing and storage of foods that ultimately contribute to their sensory characteristics. In addition to their nutritional value, food proteins, and peptides exhibit distinct biological activities Hartmann and Meisel, ; Moller et al.
BP are predominantly encrypted inside bioactive proteins Meisel and Bockelmann, By far, bovine milk Torres-Llanez et al. However, they can also be obtained from other animal sources such as bovine blood Przybylski et al. Some vegetal sources of BP and proteins are wheat Kumagai, , maize, soy Singh et al. In vivo , encrypted peptides can be liberated during gastrointestinal GI digestion by enzymes such as trypsin or by microbial enzymes.
In vitro , BP can also be released during food processing or ripening by microbial enzymes e. Lactobacillus helveticus Gobbetti et al.
4 editions of this work
BP have been identified and isolated from animal and vegetal sources and are abundantly present in protein hydrolysates and fermented dairy products. Currently, BP and nutraceutical proteins are being developed to improve human health by preventing or alleviating medical conditions such as coronary heart disease, stroke, hypertension, cancer, obesity, diabetes, and osteoporosis Gilani et al.
Peptides derived from animal proteins have been attributed to different health effects Bhat et al. Although blood disposal is a severe problem for meat processors, serum albumin, the main blood protein has received little attention. In a recent study, serum albumin was hydrolyzed using different concentrations of trypsin and the peptide sequences in the hydrolysates presented the following activities: angiotensin-converting enzyme ACE inhibition antihypertensive activity , DPP-IV inhibition glucose regulation , and antioxidation Arrutia et al. Blood obtained from the slaughterhouse is part of the meat production food chain that has not been fully exploited.
Haemoglobin fragments can have a profound physiological function. Degradation step coupled with excretion afforded shorter peptides from red blood cells. Both the primary and the secondary proteolysis products were subjected to further stepwise C - and N -terminal chain shortening, giving rise to families of closely related peptides that are found in animal tissue extracts Ivanov et al. Two excellent works on BP from vegetal sources have been recently published Malaguti et al. BP produced during in vitro GI digestion of soybean seeds and soy milk have been investigated Singh et al.
The analysis was performed on extracted protein samples from soybean seeds and milk or directly on untreated soy milk. The results indicated that soybean proteins experimented degradation during GI digestion generating a large number of BP, some with established activity, and some with predicted antimicrobial activity. Endogenous proteases were also used to investigate the presence of peptides Singh et al.
Peptides found in soy milk samples could be formed during food processing Capriotti et al. Soy hydrolysate and the soy-fermented foods, natto and tempeh, were digested with a variety of endoproteases such as pronase, trypsin, Glu C protease, plasma proteases, and kidney membrane proteases to generate oligopeptides, most likely derived from glycinin, a soy protein.
Digestion of natto with pronase provided a peptide with ACE inhibitory activity and a peptide with surface active properties. Likewise, hydrolysis of natto with kidney membrane produced a peptide with ACE inhibitory activity, and a peptide with anti-thrombotic activity which resembles hirutonin, a previously described synthetic thrombin inhibitor Gibbs et al. Cereal grains that have been used in human diets for a long time such as wheat, barley, rice, rye, oat, millet, sorghum, and corn, are a rich source of BP Malaguti et al. Scientific evidence has shown the health benefits of consuming whole grains for preventing diseases such as diabetes, cancer, and cardiovascular diseases.
Wheat and oat showed the presence of ACE inhibitory peptides and dipeptidyl peptidase inhibitor, as well as peptides with anti-thrombotic, antioxidant, hypotensive, and opioid activities. On the other hand, wheat and rice have proteins with peptidic sequences showing anticancer activity. Wheat and barley showed the greatest diversity and abundance of peptides with potential biological activity among the cereal proteins Malaguti et al.
Further research is required to establish the mechanism to release the active peptides sequences from cereal grains. They can be formed from the N -terminal amino acid residues of a linear peptide or protein and have been identified in various foods, particularly in roasted coffee, cocoa, roasted malt, chicken essence, and fermented foods such as beer, distillation residue of awamori, and aged sake.
DKPs can also be found in whey protein hydrolysates, and some beverages—therefore DKPs have been considered as a functional component. It has been reported that some DKPs found in the distillation residue of awamori show antioxidant activity Kumar et al.
Cyclo -Phe-Phe present in chicken essence acted as a dual inhibitor of the serotonin transporter and acetylcholinesterase. On the other hand, cyclo -His-Pro displayed effects such as food intake inhibition and body weight reduction in rats, therefore it might influence human biological regulation Yamamoto et al.
Food Proteins and Peptides Chemistry Functionality Interactions and Commercialization
Food industry produces a large amount of waste. For instance, as a result of olive oil extraction two different kinds of waste materials are generated: the solid waste, that is a combination of olive pulp and stone and an aqueous liquor, constituted by vegetation water, soft olive tissues, and water added during refinement. These residues are particularly polluting products that are not easily biodegradable and difficult to treat.
In a recent study, a new strategy for the recovery of waste proteins from olive seed with the potential to produce antioxidant and antihypertensive peptides has been investigated. Enzymatic hydrolysates of olive were prepared by treatment with five different proteases namely alcalase, thermolysin, neutrase, flavourzyme, and PTN. Among them, alcalase was the enzyme that yielded the hydrolysate with the highest antioxidant activity. Fractionated hydrolysates showed a high concentration of short chain peptides, with significantly higher antioxidant and antihypertensive capacities than fractions with higher MWs.
Thermolysin was the enzyme that afforded the hydrolysate with the highest ACE inhibitory capacity Esteve et al. The processing of fruits and vegetables generates a significant amount of waste material. These residues can be used for animal feeding; however, the vast majority is discarded. Stones of fruits such as plum Prunus domestica L.
The resultant extracted proteins were digested using alcalase, thermolysin, flavourzyme, and protease P enzymes and antioxidant and ACE inhibitory capacities of the hydrolysates were assayed. Alcalase was the enzyme showing the most promising extract for the isolation of antioxidant and potential antihypertensive peptides. Bovine milk, cheese, and dairy products are the greatest sources of bioactive proteins and peptides derived from food Korhonen, ; El-Salam and El-Shibiny, ; Lemes et al. Presumably, this may be one of the primary reasons why milk is required beyond nutrition in the first months of life Moller et al.
Milk proteins have a range of biological activities. For instance, immunoglobulins have an immunoprotective effect and lactoferrin Lf displays antibacterial activity. Low concentrations of growth factors and hormones, mainly present in colostrum, appear to play a significant role in post-natal development Park and Nam, The major role of milk proteins is to supply amino acids and nitrogen to the young mammals and constitute an important part of dietary proteins for the adult Sharma et al. Milk proteins are a rich source of biologically active peptides that are released during GI digestion or food processing Fitzgerald and Meisel, ; Meisel and Fitzgerald, As an example, opioid peptides that exist in dairy products have pharmacological properties similar to morphine and play an active role in the central nervous system CNS Haque et al.
Using liquid chromatography-mass spectrometry HPLC-MS and tandem mass spectrometry MS , a large number of medium and low-MW BP opioid, phosphopeptides were identified in human milk from mothers of pre- and full-term infants. The formation of many peptides confirms the greater susceptibility of human milk to casein proteolysis compared to bovine milk.
Characterization of the peptide sequence, allowed to establish the pathway of casein hydrolysis which leads to the formation of small peptides. It was found that the action of a plasmin-like enzyme acting on specific lysine residues is the primary step in casein degradation. This work reinforces the importance of maternal milk and demonstrates the difficulty to reproduce it artificially. As a consequence of the dynamic nature of maternal milk, a succession of potentially BP is produced in the intestine, which is hard to reproduce in artificial products.
Further studies are therefore required to ascertain the role of peptides derived from casein as nutritional and pharmacological factors Ferranti et al. Apart from its importance as a growth factor, Lf, an iron-binding glycoprotein present in the milk of all mammals, has antimicrobial properties and shows immunomodulating effects. Lf and Lf-derived peptides have been reported to influence cytokine production which is involved in immune and inflammatory processes of the body Moller et al. Fermentation of milk proteins using lactic acid bacteria LAB is an attractive approach to generate functional foods enriched with BP given the low cost and positive nutritional image associated with fermented milk products Hayes et al.
Consumption of fermented milk containing BP has a blood pressure—lowering effect in hypertensive subjects. Antihypertensive peptides have also been found in the whey fraction of milk protein. Peptides isolated and characterized from cow milk proteins show mineral-binding, opioid, ACE inhibitory, immunomodulatory, cytotoxicity, anti-carcinogenic, antibacterial, and anti-thrombotic activities.
Although, some variations on the nature of BP depending on the milk protein source, the isolation, and characterization of peptides of different bioactivities from milk protein hydrolyzates and products of buffalo, camel, goat, mare, sheep, and yak milk has been reported El-Salam and El-Shibiny, Daily use of fermented milk containing BP has a blood pressure—lowering effect in hypertensive subjects. A fermented milk product— L.
Among the microorganisms that have been used, Lactobacillus species, L. Presumably, these peptides are stable and are absorbed because of their small size and carboxyl-terminal proline—proline sequence, which is resistant to peptidase Seppo et al. Table 1 shows the amino acid sequence of some BP isolated from milk, as well as their bioactivity. Some examples of BP from bovine milk proteins Mohanty et al.
Navam S. Hettiarachchy (Author of Food Proteins and Peptides)
In a different work, 69 BP released from casein were identified. These sequences of amino acids were classified mainly as ACE inhibitors, opioid, and antimicrobial peptides Boutrou et al. Donkey milk is a valuable product for the food industry due to its nutraceutical, nutritional, and functional properties.
Endogenous peptides derived from donkey milk have been investigated for their antioxidant and ACE inhibitory activities. In a recent study, five peptides were prepared and their retention times and fragmentation patterns compared to the natural occurring homologs. Peptides from the permeate of bovine colostrum after dialysis or those generated by a simulated GI digest have been characterized and tested for bioactivity using murine intestinal mICc12 cells and their bioactivities compared with the bioactivity of intact colostrum. Remarkably, the most potent BP originated from non-digested colostrum, which had only been subject to endogenous protease activity Jorgensen et al.
Eggs are known as a source of valuable proteins in human nutrition and have been considered an important source of many BP Wu et al. The identification and characterization of biologically active peptides released in vitro or in vivo from egg proteins have been achieved, and the results have contributed to change the image of the egg as a new source of biologically active ingredients for the development of functional foods with specific benefits for human health and the treatment and prevention of diseases Bhat et al.
It is now well established that eggs contain numerous substances with potential and demonstrated therapeutic effects, beyond supplying basic nutritional requirements Zambrowicz et al. Research aimed to identify new and existing biological activities of hen egg components will help to define new methods to further improve the value of eggs. Egg white protein powder EWPP is a novel egg-derived product that is being increasingly applied in the food processing industry because of its long shelf life.
EWPP has been hydrolyzed by three different proteases and the enzymatic hydrolysates sequentially fractionated by ultrafiltration membranes. Among the enzymes that were used alcalase can be considered the best enzyme for the preparation of antioxidant peptides derived from egg white protein Lin et al.
The effect of cooking methods and GI digestion on the antioxidant activity of peptides derived from avian egg have been studied. The results suggest that fresh egg yolk has higher antioxidant activity than fresh egg white and whole eggs. Cooking of eggs reduced the antioxidant activity whereas simulated GI digestion increased it. Boiled egg white hydrolysate showed the highest activity and a total of 63 peptides have been identified, which indicates the formation of novel antioxidant peptides.
This results suggest the potential role of eggs as a dietary source of antioxidants Remanan and Yu, Three ovomucin hydrolysates have been prepared and desalted and only the desalted alcalase hydrolysate increased the proportion of low-MW peptides which showed anti-inflammatory activity. The showed biological activity was comparable to anti-inflammatory activity in dermal fibroblasts. This class of peptides may have potential applications for maintenance of dermal health and treatment of skin diseases Sun et al.
Meat and meat products are traditionally associated with increased risk of cancer, obesity, and other diseases, ignoring the role fact meat plays in human health. BP derived from meat products have the potential for incorporation into functional foods and nutraceuticals. Meat and fish derived peptides have been shown to exhibit antihypertensive effects in vivo , along with antioxidant capabilities and other bioactivities such as antimicrobial and anti-proliferative activities in vitro Ryan et al. However, a limited number of food products containing meat derived BP are commercially available Ryan et al.
The peptide Arg-Pro-Arg showed the greatest activity in vivo.
These results suggest that pork meat constitute a source of bioactive compounds that could be utilized in functional foods or nutraceuticals Escudero et al. Marine organisms Ngo et al. Chemical diversity is the result of the highly dynamic marine environment, and it represents an unlimited resource of new active substances with potential use as bioactive products. Marine organisms such as fish, shellfish mollusks, marine processing waste, and crustaceans are abundant sources of a myriad of structurally diverse bioactive organic compounds Aneiros and Garateix, ; Lee et al.
In Table 2 , the structures of some short peptides of marine origin, as well as the corresponding activity are represented. A well-documented evidence of their potential for human health Fan et al. BP isolated and identified from crustaceans, regulate a large number of physiological functions, including colour change, heart activity, exoskeletal and visceral muscles, metabolic function, development, metamorphosis, and reproduction.
Proteins derived from these marine organisms represent a unique source of proteins that can be used as raw materials for the generation of biofunctional peptides Kim et al. The chemistry and biological activities of BP obtained from marine algae, sponges, tunicates, ascidians, coelenterates, and mollusks have been investigated Cheung et al. In silico proteolysis and quantitative structure—activity relationship studies of marine algae-derived BP, as well as in vivo evaluation and novel technologies in BP studies and production have been reviewed Fan et al.
Macroalgae are a group of marine organisms that have developed complex and unique metabolic pathways producing a surplus of bioactive organic compounds. These include proteins, linear peptides, cyclic peptides and depsipeptides, peptide derivatives, amino acids, and amino acid-like components. Some BP derived from macroalgae proteins have been characterized; however, macroalgal proteins still represent an unexplored source of BP that can be used as functional foods to provide specific health benefits and disease-preventing properties mainly antihypertensive Harnedy and Fitzgerald, Currently, the relationship between chemical structure and activity of a peptide can not be predicted.
The activity of a peptide depends on its structure, i.
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For instance, peptides with higher ACE inhibitory activity usually have aromatic or basic N -terminal amino acids, higher quantity of hydrophobic and positively charged amino acids in C -terminal Li and Yu, To be considered bioactive, a dietary component should impart a measurable biological effect at a physiologically level. This bioactivity must have the potential to affect health in a beneficial way, which excludes potentially damaging effects such as toxicity, allergenicity, and mutagenicity Moller et al.
In Table 3 , the amino acids sequence of some peptides, along with the corresponding activity are presented. Peptides derived from milk proteins have shown antioxidant properties that prevent peroxidation of essential fatty acids. For instance, the addition of a Leu or Pro residue to the N -terminus of a His-His, dipeptide will enhance antioxidant activity and facilitate further synergy with non-peptide antioxidants [e.
On the other hand, it has been demonstrated, that digestion of casein produces phosphorylated peptides that exhibit both hydrophilic and lipophilic antioxidant activity due to both metal ion sequestering and quenching of ROS Clare and Swaisgood, To use these wastes, and to add value to several underutilized fish species, protein hydrolysates from fish proteins are being prepared using enzymes. These fish protein hydrolysates contain small BP with antioxidant activity Elias, The antioxidant potential of protein hydrolysates depends on the amino acid composition and on the disruption of the tertiary structure of parent proteins by enzymatic hydrolysis that results in increasing the solvent accessibility of oxidatively labile amino acid residues.
The antioxidant activities of water-soluble fractions of a Spanish dry-cured ham extract of a fractionated peptide extract by size-exclusion chromatography have been described. The combination of antihypertensive and antioxidant capacities could help to reduce the adverse effect of NaCl, an ingredient commonly used in these products Escudero et al.
Soy peptides have shown increased antioxidant activities Singh et al. Soy protein hydrolysates prepared from native and heated soy protein isolates using different enzymes had varying degrees of hydrolysis 1. The first tripeptide displayed the highest DPPH radical scavenging activity and, presumably, the presence of the amino acids His-Tyr sequence could contribute significantly to the antioxidant activity of the peptides Bougatef et al. Enzymatic hydrolysates from wheat germ protein Zhu et al. Antioxidant proteins and peptides have also been identified in egg Sakanaka and Tachibana, , potato, and gelatin Je et al.
The presence of antioxidant peptide segments in proteins may help to explain why dietary protein intake can promote animal and human health beyond the standard nutritional benefits exerted Elias et al. Digestion studies in vitro have provided evidence that a mixture of peptides 2—4 amino acid residues obtained from certain food proteins using human digestive enzymes under physiological conditions possess potent antioxidant activity Zhu et al.
Shellfish is another potential source for antioxidant peptide production in the GI system Ngo and Kim, The GI digests of oyster Crassostrea gigas yielded an active 1. This peptide inhibited peroxidation of lipids and neutralized hydroxyl and superoxide radicals Ngo and Kim, Alaska pollock frame protein is normally discarded as an industrial by-product in the processing of fish.
Another peptide with 16 amino acid residues 1. Oxidation is one of the leading causes of diseases and pathogenesis in humans. Melatonin, N -acetylmethoxytryptamine, can protect cells against oxidation Xiong, The endogenous dipeptide cyclo His-Pro that is present in the CNS and several body fluids and the GI tract, has a neuroprotective role. In vitro studies on rats have demonstrated that cyclo His-Pro enhances the cellular antioxidant capacity as well as the expression of small heat shock proteins. Additionally, there is some evidence that cyclic dipeptide has a role in ameliorating diabetes Minelli et al.
Peptides derived from milk proteins have also shown antioxidant activity to prevent peroxidation of essential fatty acids. The addition of a Leu or Pro residue to the N -terminus of a His-His, dipeptide will enhance antioxidant activity and facilitate further synergy with non-peptide antioxidants e. BHT Kitts and Weiler, It has been demonstrated that many peptides and protein hydrolysates from plant and animal origin possess antioxidant activity.
For example, peptides derived from soy protein Wang and De Mejia, ; Singh et al. Antioxidant peptide fragments containing tyrosine and methionine had substantial radical-scavenging activity and played a significant role in the overall antioxidant activity of the protein hydrolysates Torkova et al. The antioxidant activity of several protein hydrolysates and peptide mixtures has been tested in situ and some of them have been already used as ingredients in commercial food processing. Whey, casein, soy, potato, and yolk protein hydrolysates have been shown to inhibit lipid oxidation in muscle foods Wang and Xiong, These peptides were chemically synthesized, and showed antioxidant activity in radical scavenging assays.
The strategy utilized in the investigation proved to be suitable for quick, sensitive, and accurate analysis of complex protein hydrolysates Liu et al. Proteins of goat milk were hydrolyzed by pepsin into caseins GCP , whey proteins GWP and protein fractions containing multiple soluble peptides. Proteins and peptides derived from goat milk have also received increased attention, particularly the BP released from the parent proteins by digestive enzymes that showed reduced allergenicity compared to bovine milk.
The generated peptides were examined for radical scavenging activities. The results demonstrate that soluble peptides obtained by digestion with pepsin possess remarkable ability to scavenge superoxide radicals and thus providing an interesting opportunity for their potential candidacy as antioxidant BP Ahmed et al. Antimicrobial peptides AMPs are an abundant and diverse group of molecules that are produced by many tissues and cell types in a variety of invertebrate, plant, and animal species.
Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers Brogden, These peptides are involved in the inhibition of cell growth and in the killing of several microorganisms, such as bacteria and fungi. Antimicrobial peptides are usually below a MW of 10 kDa and encoded within the sequences of native protein precursors, may also be generated in vitro by enzymatic hydrolysis Kim and Wijesekara, AMPs constitute a promising alternative as therapeutic agents against various pathogenic microbes Cruz et al.
More than 60 peptide drugs have reached the market for the benefit of patients and approximately peptide therapeutics are currently being evaluated in clinical trials Fosgerau and Hoffmann, AMPs can be classified into three families according to different structural features: 1. Most of these peptides adopt an amphipathic structure with both cationic and hydrophobic properties that facilitate their interaction with anionic cell walls and membranes of microorganisms Pimenta and De Lima, Four linear AMPs were isolated from the venom of the primitive scorpion Opisthacanthus madagascariensis.
From Hymenoptera venom, antimicrobial peptides have been described in wasps 19 , bees, and ants. AMPs have been described from the venom of wolf spiders Lycosa singoriensis , Lycosa carolinensis , Lycosa erythrognatha , and Oxyopes kitabensis Pimenta and De Lima, Marine-derived antimicrobial peptides are well described in the haemolymph of the many marine invertebrates Tincu and Taylor, Casein Derived Antibacterial Peptides show inhibitory activity against Streptococcus mutans , Streptococcus sanguis, Porphyromonas gingivalis , Streptococcus sobrinus , Sthaphylococcus aureus , Escherichia coli , and Salmonella typhimurium.
On the other hand, Lf a Whey Protein Derived Antibacterial Peptide shows bacteriostatic effects in vivo and in vitro against Bacillus stearothermophilus, B. XLAsp-P1 has a remarkable in vitro potency against Gram-positive and Gram-negative bacteria and potent inhibitory activity against breast cancer cells. The use of transmission electron microscopy, allowed to understand the mechanism of action of this novel peptide.
The antimicrobial activity is based on the destruction of the cell membrane Li et al. Bovine coagulated blood, a slaughterhouse by-product, has been described as a rich source of antimicrobial peptides. The — peptide also inhibited the microbial growth under refrigeration during 14 days. These antimicrobial effects were close to those of the BHT Przybylski et al. Immunomodulatory peptides derived from hydrolysates of rice and soybean proteins act to stimulate reactive oxygen species ROS , which triggers non-specific immune defence systems. The anterior pituitary AP contains a variety of BP such as: brain-gut peptides, growth factors, hypothalamic releasing factors, posterior lobe peptides, opioids, and various other peptides.
The release of peptides from the AP cell, the synthesis, storage and release have been described. Since AP peptides are produced in low quantities, endocrine activity has not been established. There is some evidence for paracrine, autocrine, or intracrine roles in growth, differentiation, and regeneration, or in the control of hormone release Houben and Denef, Ngo et al.
Celiac disease is a genetic autoimmune disorder consisting in the damage of the small intestine after the ingestion of gluten. The roles of the many BP in the pathogenesis of celiac disease remain unclear. An increase in insulin concentrations in individuals with celiac disease has been observed, but further studies are required to determine whether increased insulin concentrations is related to an increased risk for hyperinsulinemia Janas et al. Proteins and peptides from egg, milk, soy, and plant sources have shown anti-inflammatory properties.
Ovotransferrin is an egg white protein well known for its antibacterial activity Wu et al. It is often present in large amounts in chickens, during inflammation and infection processes. This protein also has immunomodulating effects on chicken macrophages and heterophil-granulocytes and can inhibit proliferation of mouse spleen lymphocytes Xie et al.
Immunomodulatory peptides derived from hydrolysates of rice and soybean proteins act to stimulate ROS, which triggers non-specific immune defence systems. The molecular diversity of marine peptides, as well as information about their anti-inflammatory properties and mechanisms of action, have been described, along with the anti-inflammatory effects of novel BP from sponges, bacterium, and microalgae Kim et al.
The anti-inflammatory, anti-hemolytic, antioxidant, anti-mutagenic, and antimicrobial activities of crude extracts and peptide fractions obtained from fermented milks with specific Lactobacillus plantarum strains was carried out. Crude extracts showed higher activity than both peptide fractions in most of the activities assessed.
In particular, L. These results provide valuable evidence of multifunctional role of peptides derived of fermented milk by the action of specific L. In an attempt to identify the shortest peptide possessing the full anti-inflammatory activity of the native protein, a number of SV-IV oligopeptides, whose sequences were derived from the N -terminal segment of the protein, were prepared by Fmoc chemistry and their anti-inflammatory properties were evaluated. Purification and identification of anti-inflammatory peptides derived from simulated GI digests of velvet antler protein Cervus elaphus Linnaeus has been performed.
These results suggested that the peptides derived from velvet antler protein could potentially be used as a promising ingredient in functional foods or nutraceuticals against inflammatory diseases Zhao et al. Antihypertensive peptides, also known as ACE inhibitors have been derived from milk, corn, and fish protein sources Kim et al. ACE is essential for the regulation of blood pressure Borer, ACE catalyzes the transformation of angiotensin I to potent vasoconstrictor angiotensin II and the degradation of the vasodilator, bradykinin.
Structure-activity correlations among different peptide inhibitors of ACE indicate that binding to ACE is strongly influenced by the C -terminal tripeptide sequence of the substrate. ACE appears to prefer substrates or competitive inhibitors which mainly have hydrophobic aromatic or branched side chains amino acid residues at the three C -terminal positions Gobbetti et al.
Several tripeptides that inhibit ACE have been isolated from foods. The milk-derived bioactive tripeptides Val-Pro-Pro and Ile-Pro-Pro reduced blood pressure in mildly hypertensive subjects Tuomilehto et al. There is some evidence that the ingestion of sour milk fermented by L. Long-term administration of Ile-Pro-Pro and Val-Pro-Pro has been shown to prevent the development of hypertension in rats and to reduce BP by a single oral administration Tuomilehto et al.
Since ACE inhibitory peptides can be obtained by the action of enzymes on complete proteins in vitro during food processing and in vivo through GI digestion, peptides that inhibit ACE may be generated in or incorporated into functional foods to develop useful health products. Some products containing peptides with ACE inhibitory properties are being investigated, or some are already in the market, but further studies to validate their efficiency are required Murray and FitzGerald, In a different study, rice protein was hydrolyzed by alcalase and the resulting hydrolysate was tested for ACE inhibitory activity in vitro.
The antihypertensive effect of rice protein hydrolysate was also investigated in SHR showing an IC50 value of 0. The commercially available Food for Specified Health Uses FOSHU products containing small peptides: tryptic hydrolysate of casein, Katsuobushi oligopeptide, the aqueous extract from Mycoleptodonoide saitchisonii, sour milk, sardine peptide, seaweed peptides, and sesame peptides inhibit the ACE enzyme.
However, the efficacy of peptide intake for borderline hypertensives still requires further investigation. For a long time, macroalgae have been a key component of the diet of East Asian populations. It is also a source of functional and technological ingredients in the food, pharmaceutical, and cosmetic industries Pal et al. The protein from the red alga Palmaria palmate was extracted and hydrolyzed with the enzyme papain to generate renin inhibitory peptides, whose sequences were elucidated.
The synthesized peptide was also subjected to in silico cleavage analysis using the computer program Expasy peptide cutter and hydrolyzed using enzymes found in the GI tract to release dipeptides and tripeptides. These results suggest that this propeptide and the dipeptides and tripeptides freed from it may cross the lumen into the bloodstream and potentiate an antihypertensive effect Fitzgerald et al. The cereals wheat, oat, barley and rice have been evaluated for BP showing high occurrence frequencies of ACE-inhibitor peptides as well as of dipeptidyl peptidase-inhibitor and anti-thrombotic, antioxidant, hypotensive, and opioid activity.
Wheat and rice proteins presented sequences with anticancer activities. Wheat and barley showed the greatest diversity and abundance of potential biological activity among the cereal proteins. Further research needs to be conducted to learn how these biologically active peptide sequences are released from cereal grains Cavazos and Gonzalez de Mejia, A few BP have been tested in human trials. The available data indicates that bioactive tripeptides with antihypertensive activities reduce the risk of elevated blood pressure in subjects with moderate hypertension Cicero et al. BP can be used to design prevention strategies.
Milk BP may be employed in the prevention of risks in metabolic syndrome MS and its complications via the regulation of blood pressure, the uptake of free radicals, and the control of food intake. Studies on potentially hypotensive milk protein hydrolysates illustrate the significant difference between allergenicity and immunogenicity. Despite the existence of data on the relationship between the structure of food proteins and peptides derived from food, the assessment of the allergenic properties of products derived from an allergenic source is not straightforward Reddi et al.
A large number of proteins and peptides of plant and animal origin are known to exhibit cytotoxic effects. There is evidence that many cytotoxic compounds described in the literature exclusively affect malignant cells leading to the assumption that a cancer protective effect could exist for such bioactive proteins and peptides. All the constituents that are responsible for the allergenicity Hartmann et al. Some protein breakdown products, i. Despite the existence of data on the relationship between the structure of food proteins and peptides derived from food, the assessment of the allergenic properties of products derived from an allergenic source, is not straightforward Reddi et al.
The endogenous ligands for opioid receptors are peptides, also known as endorphins. These peptides share the common N -terminal sequence of Tyr-Gly-Gly-Phe- Met or Leu , which has been termed the opioid motif ; this is followed by various C -terminal extensions yielding peptides ranging from 5 to 31 residues in length Aldrich, Due to the importance of mu opioid receptor MOR agonists such as morphine as analgesics, the primary focus has been for the treatment of pain.
The emphasis for opioid peptide analog development has been to induce analgesia through activation of opioid receptors in the CNS. ADAMB was 4- and fold more potent as an analgesic than morphine following oral and s. BP derived from milk proteins may function as exorphins or formones food hormones. Although this role needs further clarification, pharmacological properties similar to morphine and naloxone inhibitable properties have been shown Gobbetti et al.
Casomorphins may produce analgesia, modulate social behaviour, influence postprandial metabolism by stimulating the secretion of insulin and somatostatin, and may influence GI absorption of nutrients by prolonging the GI transit time and exerting an antidiarrhoeal effect Meisel and Schlimme, Peptides with opioid activities Aldrich, ; Yamamoto et al.
Exorphins or opioid peptides derived from food proteins such as wheat and milk e. A potential target for food protein-derived BP is calmodulin CaM , a protein that plays important roles in maintaining physiological functions of cells and body organs Chung et al. CaM is a calcium-binding protein formed by amino acid residues with a weight of This protein plays multifunctional roles in the translation of intracellular messages Klee and Vanaman, Some of the functions of CaM include calcium-dependent cell division, cell proliferation, and neurotransmission Rasmussen and Means, Excessive levels of CaM can have a detrimental effect on the body and may lead to the development of chronic diseases such as cancer.
Flaxseed proteins have hydrophobic and positively charged amino acids that could enhance the production of CaM-binding peptides through enzymatic hydrolysis. Hydrolysis of flaxseed proteins with alcalase, afforded low-MW peptides Omoni and Aluko, Similarly, hydrolysis of pea proteins with alcalase produced CaM-binding peptides Li and Aluko, MS consists of a deadly quintet of factors, namely diabetes, centripetal obesity, hypertension, dyslipidemia elevated triglycerides, dense low-density lipoproteins, and low high-density lipoproteins , and alterations in the thrombotic potential that are related to hyperinsulinemia and insulin resistance Hollander and Mechanick, Peptides structurally related to the insulin receptor IR -binding protein mcIRBP have been identified in various plants that have IR kinase-activating abilities similar to mcIRBP that has a proved blood glucose-lowering activity that exhibits IR-binding potentials Lo et al.
Some studies have shown that dietary proteins—especially milk proteins—could be a natural source of these enzymes. The beneficial effects of these inhibitory peptides can be explained through several mechanisms, such as the satiety response, regulation of incretin hormones, insulinemia levels, and reducing the activity of carbohydrate degrading digestive enzymes Patil et al. The extraction of peptides from egg yolk with a non-commercial enzyme obtained from Asian pumpkin has been described.
These peptides remaining after phospholipid removal, and their four synthetic analogs were investigated. This peptide also showed the highest antioxidant activity as a free radical scavenger Zambrowicz et al. Soy protein is of particular interest because can be utilized as an aid to treat MS. Its relation to several health benefits, including weight loss and prevention of complications related to cardiovascular risk factors, as well as the improvement of lipid profile and glucose and insulin homeostasis has been documented Velasquez and Bhathena, Animal models have demonstrated that soy protein has a positive effect on weight and fat loss that was especially prominent when comparing casein-based diets to soy-based foods.
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Nutraceuticals are substances of natural origin that can be extracted from various sources e. In recent years, functional foods and nutraceuticals have attracted much attention, particularly for their impact on human health and prevention of certain diseases Meisel, ; Lee et al. Considering that most functional peptides are present in complex matrices containing a large number of hydrolyzed protein fractions, their separation and purification are required.
Conventional pressure-driven processes can be used for amino acids and peptides separation but are limited by their fouling problems and their low selectivity when separating similar sized biomolecules Bazinet and Firdaous, Processes combining an electrical field as a driving force and porous membranes have been developed for the separation of biopeptides to obtain better-purified products.
More recently, electrodialysis using ultrafiltration membranes has been developed to fractionate simultaneously acidic and basic peptides using a conventional electrodialysis cell, in which some ion exchange membranes are replaced by ultrafiltration ones Bazinet and Firdaous, After separation and identification of BP in three hypoallergenic infant milk formulas, the identity of 24, 30, and 38 BP was confirmed in each of the three infant milk formulas.
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