Bioactive Protein Hydrolysates Research Articles

Bioactive Peptides and Protein Hydrolysates Used in Meat and Meat Products’ Preservation─A Review

Bioactive Peptides and Protein Hydrolysates Used in Meat and Meat Products’ Preservation─A Review

Valorization of Malaysian Fish Sausage (Keropok Lekor) By-Products into Bioactive Fish Protein Hydrolysate by Bacillus licheniformis Fermentation: Influence of By-Products Characteristics on Nutritional, Antioxidant, and Antibacterial Capacities

Valorization of Malaysian Fish Sausage (Keropok Lekor) By-Products into Bioactive Fish Protein Hydrolysate by Bacillus licheniformis Fermentation: Influence of By-Products Characteristics on Nutritional, Antioxidant, and Antibacterial Capacities

Enzymatic processing of animal by-products: production of antioxidant hydrolysates with Bacillus sp. CL18 crude protease.

Protein hydrolysates might display diverse bioactivities with potential relevance to human and animal health and food technology. Enzymatic hydrolysis of agro-industrial by-products is increasingly focused. In this study, a crude protease from Bacillus sp. CL18 was applied to obtain antioxidant protein hydrolysates from porcine, bovine, poultry, and fish by-products. The crude enzyme hydrolyzed all the twelve investigated by-products, as detected by increased soluble protein contents after 4h of proteolysis. Hydrolysates exhibited higher radical-scavenging, Fe2+-chelating and reducing power capacities than non-hydrolyzed by-products. Hydrolysis times (0-8h) and enzyme-to-substrate (E/S) ratios (384, 860, and 1,400 U/g) were assessed to produce antioxidant bovine lung hydrolysates. The highest E/S ratio accelerated both hydrolysis and increases in antioxidant activities; however, it did not result in bioactivities higher than hydrolysates obtained with the intermediate E/S ratio. Optimal antioxidant activities could be reached after 6h of hydrolysis using 860 U/g. Animal by-products are interesting sources of bioactive protein hydrolysates, which could be produced with a non-commercial bacterial protease. This might represent a promising strategy for the valorization of animal by-products generated in large amounts by the agri-food sector.

Effect of hydrolysis degree with Alcalase on antioxidant and antigenic properties of whey and colostrum protein hydrolysates

Enzymatic hydrolysis of dairy proteins is aimed to increase their nutritional value and reduce their allergenic properties. It is relevant to study the effects of enzymatic hydrolysis with highly active endopeptidase alсalase on the bioactivity of the whey and colostrum protein components. Dairy hydrolysates with various degree of Alcalase treatment were obtained in the present study. A comparative analysis of cleaved dairy proteins and their peptide fractions with a 5 and 10 kDa cutoff was performed. The protein and peptide composition of hydrolysates was determined using various techniques. The bioactivity of hydrolyzed whey and colostrum samples were estimated. The antioxidant activity of hydrolyzed and fractionated (5 kDa cutoff) whey samples increased by 5.91/6.62-fold and that of colostrum by 14.22/7.24-fold in fluorimetric/spectrophotometric assay, respectively. A significant decrease in the antigenic potential of milk peptides was observed with increasing degree of hydrolysis and subsequent ultrafiltration. Thus, bioactive dairy protein hydrolysates were obtained, which are applicable as a component of specialized foods with proven hypoallergenic properties and high antioxidant activity.

Protein Hydrolysates from Fishery Processing By-Products: Production, Characteristics, Food Applications, and Challenges.

Fish processing by-products such as frames, trimmings, and viscera of commercial fish species are rich in proteins. Thus, they could potentially be an economical source of proteins that may be used to obtain bioactive peptides and functional protein hydrolysates for the food and nutraceutical industries. The structure, composition, and biological activities of peptides and hydrolysates depend on the freshness and the actual composition of the material. Peptides isolated from fishery by-products showed antioxidant activity. Changes in hydrolysis parameters changed the sequence and properties of the peptides and determined their physiological functions. The optimization of the value of such peptides and the production costs must be considered for each particular source of marine by-products and for their specific food applications. This review will discuss the functional properties of fishery by-products prepared using hydrolysis and their potential food applications. It also reviews the structure-activity relationships of the antioxidant activity of peptides as well as challenges to the use of fishery by-products for protein hydrolysate production.

Antimicrobial and Antioxidant Properties of Bovine Livers and Hearts Hydrolysates

Our previous research has indicated that bioactive protein hydrolysates derived from porcine by-products possess the potential to be utilized in the production of functional additives and food supplements. The objective of this investigation was to assess the antioxidant and antimicrobial characteristics and amino acid changes in hydrolysates of lyophilized meat of bovine livers and hearts. The relevant enzymes, papain and pepsin, were used to hydrolyze the meat by-products over periods of 3, 6, and 24 h. The antimicrobial properties of all enzymatically digested samples were assessed against Listeria monocytogenes, Bacillus cereus, Salmonella enterica subsp. enterica Serovar Typhimurium. Bacillus cereus, and Escherichia coli, S. aureus subsp. aureus. The assessment of antiradical activity involved the quantification of DPPH• and ABTS•+ absorbance in bovine by-product hydrolysates. The hydrolysates were subjected to amino acid analysis using AccQ Tag technology, which was performed by Waters Corporation in Milford, MA, USA. The bacteria L. monocytogenes had the highest antibacterial activity (inhibition zone) (20.00 ± 0.20 mm) and less against E. coli (10.00 ± 0.10 mm) of bovine heart hydrolysates and were prepared for 24 h with papain. The highest values of ABTS•+ (98.1 ± 0.30%) and of DPPH• scavenging activity (92.56 ± 0.56%) of cationic radicals were evaluated in the bovine liver hydrolysates after the effect of papain for 24 h. Longer hydrolysis time influenced the decrease in free hydrophobic amino acids (Ala, Val, Ile, Leu, Tyr, Phe, Pro, Met). The results confirmed the potential use of bovine liver and heart hydrolysates as functional or biologically active materials.

Çaça (Sprattus sprattus, L., 1758) Protein Hidrolizatının Fizikokimyasal Özellikleri ve Alabalık (Oncorhynchus mykiss, Walbaum, 1792) Filetolarında Kaplama Malzemesi Olarak Kullanımı

Trout is the most widely cultivated and traded fish species in Turkey and many European countries, and a total of 471686 tons of production was realized in Turkey’s seas and inland waters in 2021. In addition to its nutritive value, this fish takes a crucial position in the aquaculture sector due to its continuous and intensive production. In this study, innovative bioactive protein hydrolysates (PH) produced from sprat were used as a coating to increase the quality and shelf life of trout fillets stored at +4 ˚C. The yields of traditional hydrolysate (TH) and ultrasound-assisted hydrolysate (UH) were 8.66% and 12.63%, respectively. Protein values of TH and UH were 75.88 and 74.45%, respectively. Three fillet groups were prepared from trout: uncoated control group (C), traditional enzymatic protein hydrolysate coated group (THC), and ultrasound-assisted enzymatic protein hydrolysate coated group (UHC). TVB-N value, which was 12.96 mg/100g in fresh trout, exceeded the consumable limit with 38.52 mg/100g on the 9th day of storage in the C. This value reached 32.92 mg/100g and 33.62 mg/100g on the 12th day for THC and UHC, respectively. At the beginning of storage, 0.21 mg MA/kg TBA reached the consumable limit with 7.72 mg MA/kg in the C on the 9th day, while THC and UHC remained within the limit with 6.67 mg MA/kg and 6.79 mg MA/kg, respectively. Total aerobic mesophilic bacteria (TAMB) and total aerobic psychrophilic bacteria (TAPB) counts on day 0 of storage were 2.13 log cfu/g and 1.66 log cfu/g, respectively. These values were calculated as 6.90, 5.20, 5.04, 6.95, 3.48, and 3.22 log cfu/g for C, THC, and UHC on the 12th day of storage, respectively. The application of ultrasound during the production of protein hydrolysate significantly increased the yield and hydrolysis degree of UH compared to TH. The lipid ratio of UH was also found to be significantly lower than TH. In these respects, the application of ultrasound has provided an advantage. Although both coatings have provided significant protection compared to the C, generally similar results were obtained between the THC and UHC. PH coatings delayed the chemical, physical, and microbial spoilage of trout fillets and extended the storage period. The results showed that PH can be used as a coating on fish fillets stored in cold conditions.

Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors.

Lipoxygenases are non-heme iron-containing enzymes that catalyze the oxidation of polyunsaturated fatty acids, resulting in the production of lipid hydroperoxides, which are precursors of inflammatory lipid mediators. These enzymes are widely distributed in humans, other eukaryotes, and cyanobacteria. Lipoxygenases hold promise as therapeutic targets for several human diseases, including cancer and inflammation-related disorders. Inhibitors of lipoxygenase have potential applications in pharmaceuticals, cosmetics, and food. Bioactive peptides are short amino acid sequences embedded within parent proteins, which can be released by enzymatic hydrolysis, microbial fermentation, and gastrointestinal digestion. A wide variety of bioactivities have been documented for protein hydrolysates and peptides derived from different biological sources. Recent findings indicate that protein hydrolysates and peptides derived from both edible and non-edible bioresources can act as lipoxygenase inhibitors. This review aims to provide an overview of the current knowledge regarding the production of anti-lipoxygenase protein hydrolysates and peptides from millet grains, chia seeds, insects, milk proteins, fish feed, velvet antler blood, fish scales, and feather keratins. The anti-lipoxygenase activities and modes of action of these protein hydrolysates and peptides are discussed. The strengths and shortcomings of previous research in this area are emphasized. Additionally, potential research directions and areas for improvement are suggested to accelerate the discovery of anti-lipoxygenase peptides in the near future.

Encapsulation of Bioactive Peptides by Spray-Drying and Electrospraying.

Bioactive peptides derived from enzymatic hydrolysis are gaining attention for the production of supplements, pharmaceutical compounds, and functional foods. However, their inclusion in oral delivery systems is constrained by their high susceptibility to degradation during human gastrointestinal digestion. Encapsulating techniques can be used to stabilize functional ingredients, helping to maintain their activity after processing, storage, and digestion, thus improving their bioaccessibility. Monoaxial spray-drying and electrospraying are common and economical techniques used for the encapsulation of nutrients and bioactive compounds in both the pharmaceutical and food industries. Although less studied, the coaxial configuration of both techniques could potentially improve the stabilization of protein-based bioactives via the formation of shell-core structures. This article reviews the application of these techniques, both monoaxial and coaxial configurations, for the encapsulation of bioactive peptides and protein hydrolysates, focusing on the factors affecting the properties of the encapsulates, such as the formulation of the feed solution, selection of carrier and solvent, as well as the processing conditions used. Furthermore, this review covers the release, retention of bioactivity, and stability of peptide-loaded encapsulates after processing and digestion.

Value addition ofSamia ricini (Eri) pupae derived proteins: production and characterisation of antioxidant, ACE and DPP-IV inhibitory hydrolysates

This study aims to validate the production of multifunctional peptides from indigenously available edible nonmulberry silkworm (Samia ricini) pupae under the effect of specific enzymatic hydrolysis settings, simulated gastric and intestinal fluids. Eri pupae proteins comprising 40.81% constituents with molecular weight (MW)>10 kDa and 48.68% within 10-3 kDa are most preferable substrates for alcalase and thermolysin among other enzymes; based on the effect of relationships between 0.5-3.0% enzyme/substrate ratios and 0-24 h of hydrolysis period on rate of hydrolysis, reduced Km value (6.07 mg/ml) of alcalase and higher kcat/Km value (0.42 ml/mg/min) demonstrated by thermolysin. hydrolysates demonstrating the best angiotensin converting enzyme (ACE) inhibition (alcalase hydrolysate, 3.0%, 3 h (H1′), papain hydrolysate, 3.0%, 5 h (H2′), pepsin hydrolysate, 3.0%, 5 h (H3′)), DPPH scavenging potential (H1′ and H3′), ABTS scavenging capacity (H2′, H3′ and thermolysin hydrolysate, 3.0%, 5 h (H4′)) and DPPIV inhibition (H4′) were selected and compared their stability and peptides behaviour under gastrointestinal environment with non-hydrolysates. This study has provided enough evidence that there exists an opportunity to utilise H3′ and H4′ for practical application due to its maintenance of ACE and DPP-IV inhibition potential after digestion compared to whole Eri pupae flour or its concentrate. Thus, this preliminary scientific segment of allegation suggested that the possibility of exploration of sericulture industry derivatives through enzymatic processing not only helps in waste procurement but will also provide the opportunity to innovate cost-effective value-added products in the form of bioactive protein hydrolysates.

Production and in vitro studies of Bitter Gourd (Momodica charantia) seed protein hydrolysates with antidiabetic activity

Diabetes mellitus is a multifactorial chronic disease that affects the human population and it is the third most common cause of death worldwide. Momordica charantia is commonly known as Bitter melon, Bitter guard and used as a food and natural medicine. The scientific name, Momordica means "to bite," in Latin which is refers to the jagged edges of the leaves. Including fruits, all parts of the plant, contains a bitter compound, momordicinso and very bitter in taste. It has long been used as a traditional medicine for some ailments. Its high protein content (35.18%) makes it a promising candidate as a source of bioactive protein hydrolysates. In this study, the potential of enzymatically hydrolyzed Bitter guard seed protein to generate functional bioactive peptides was evaluated. Bitter guard seed protein concentrate was hydrolyzed using three different proteolytic enzymes (Alcalase, Bromelain, and Papain) at their respective optimum pH and temperature. The choice of enzyme affected the bioactivities to a certain degree as Bitter guard seed were shown to possess high antidiabetic activity. Bromelain Bitter guard seed protein hydrolysate showed the highest DPP-IV inhibitory activity with 79.27% inhibition, α-Glucosidase inhibitory activity with 72.15% inhibition and α-Amylase inhibitory activity with 59.98% compared to other enzymatic hydrolysates, and therefore was chosen for further investigation of its antidiabetic activity.

Bioactive protein hydrolysates obtained from amaranth by fermentation with lactic acid bacteria and Bacillus species

Protein hydrolysates are a promising source of bioactive peptides. One strategy by which they can be obtained is fermentation. This method uses the proteolytic system of microorganisms to hydrolyze the parental protein. Fermentation is a little-explored method for obtaining protein hydrolysates from amaranth. Different strains of lactic acid bacteria (LAB) and Bacillus species isolated from goat milk, broccoli, aguamiel, and amaranth flour were used in this work. First, the total protein degradation (%TPD) of amaranth demonstrated by the strains was determined. The results ranged from 0 to 95.95%, the strains that produced a higher %TPD were selected. These strains were identified by molecular biology and were found to correspond to the genera Enterococcus, Lactobacillus, Bacillus, and Leuconostoc. Fermentation was carried out with amaranth flour and the selected strains. After this process, water/salt extracts (WSE) containing the released protein hydrolysates were obtained from amaranth doughs. The peptide concentration was measured by the OPA method. The antioxidant, antihypertensive and antimicrobial activity of the WSE was evaluated. In the FRAP test, the best WSE was LR9 with a concentration of 1.99 μMTE/L ± 0.07. In ABTS, 18C6 obtained the highest concentration with 19.18 μMTE/L ± 0.96. In the DPPH test, there was no significant difference. In terms of antihypertensive activity, inhibition percentages ranging from 0 to 80.65% were obtained. Some WSE were found to have antimicrobial properties against Salmonella enterica and Listeria monocytogenes. Fermentation of amaranth with LAB and Bacillus spp. allowed the release of protein hydrolysates with antioxidant, antihypertensive, and antimicrobial activity.

A review of bioactive peptides as functional food ingredients: mechanisms of action and their applications in active packaging and food quality improvement.

The creation of bioactive peptides (BPs) from dietary proteins holds considerable promise for the expansion of functional foods and nutraceuticals. BPs have a variety of important roles in the living body, including antioxidative, antimicrobial, immunomodulatory, hypocholesterolaemic, antidiabetic, and antihypertensive properties. To preserve the quality and microbiological safety of food items, BPs have been used as food additives. Additionally, peptides may be employed as functional components in the treatment or prevention of chronic and lifestyle-related disorders. This article's main goal is to draw attention to the functional, dietary, and health advantages of using BPs in food items. Therefore, it examines the mechanisms of action and medicinal uses of BPs. This review also focuses on various uses of bioactive protein hydrolysates for enhancing food items' quality and shelf life as well as for bioactive packaging. Researchers interested in physiology, microbiology, biochemistry, and nanotechnology, as well as members of the food business, are advised to read this article.

Protein Characteristics and Bioactivity of Fish Protein Hydrolysates from Tra Catfish (Pangasius hypophthalmus) Side Stream Isolates.

Enzymatic hydrolysis is a novel method to recover highly potent bioactive fish protein hydrolysates (FPHs) from fish processing side-streams. The common way of producing FPHs directly from fish side-streams may be inappropriate due to the excess of lipids and pro-oxidants, especially in lipid-rich streams, as obtained from Tra catfish. This study aimed to optimise the hydrolysis conditions for a commercial enzyme (Alcalase® 2.4 L) (enzyme concentrate, temperature, and time) in FPH production from the fish protein isolate obtained from Tra catfish dark muscle (DM-FPI) using the pH-shift method. The degree of hydrolysis (DH), protein recovery (PR), and antioxidant properties, including DPPH radical scavenging activity (DPPH-RSA) and total reducing power capacity (TRPC), were measured to evaluate the effects of the hydrolysis conditions on the FPHs. Optimal hydrolysis was obtained at an enzyme/substrate protein ratio of 3% (v/w) and a hydrolysis temperature of 50 °C for 3 h. The FPHs obtained from different substrates, including DM-FPI, abdominal cut-off (ACO) FPI, and head and backbone blend (HBB) FPI, had similar DHs under these optimum conditions, ranging from 22.5% to 24.0%. However, the FPH obtained from abdominal cut-off isolate (ACO-FPH) showed the highest PR of 81.5 ± 4.3% and the highest antioxidant properties, with a DPPH-RSA of 86.1 ± 1.6% and a TRPC of 6.4 ± 0.4 equivalent mg vitamin C/g protein. The resulting FPHs present a natural source of antioxidants with great potential for food applications, especially the ACO-FPH. In addition, all FPHs had excellent amino acid profiles, indicating strong potential for their use as supplements. Tra catfish protein-rich side-streams can thus be processed into high-value bioactive FPHs using Alcalase for human consumption.

Edible freshwater snail (Paludomas conica) attenuates STZ‐induced diabetic complications by regulating PFK‐1 and PON‐1 gene expression

SummaryFreshwater invertebrates, especially molluscs, have recently piqued the interest of researchers as a potential new source of food protein hydrolysates. This study prepared bioactive protein hydrolysates (PPh) from the freshwater snail Paludomas conica and investigated their antioxidant and antidiabetic effects by evaluating biochemical and molecular approaches. The DPPH free radical assay, ABTS scavenging assay, FRAP assay and superoxide scavenging assay investigated the antioxidant effects. The antidiabetic potential was measured in α‐amylase and α‐glucosidase inhibition assays followed by in vivo assay in streptozotocin (STZ)‐induced diabetic animal model and gene expression studies. In all antioxidant experiments, the half‐maximal inhibitory concentration (IC50) of PPh was less than the cut‐off value, 1000 μg/mL. The inhibitory concentration of PPh was 1.89 mg/mL for α‐amylase and 334.70 μg/mL for α‐glucosidase in vitro assay. Furthermore, in the streptozotocin‐induced Wistar albino rats model of six groups (n = 5, body weight 180–20 g, age 6–7 weeks), the administration of PPh 250 mg/kg for diabetic rats a 4 weeks intervention attenuated elevated glucose levels and other diabetes‐related biomarkers (alanine aminotransferase, aspartate aminotransferase, lipid profile, total protein, uric acid). Molecular assay by the qPCR analysis showed a significant (P < 0.05) upregulation of the relative mRNA expression of antioxidant and glucose metabolism‐regulating enzymes‐related genes of superoxide dismutase (SOD‐1), Paraoxonase‐1 (PON1) and Phosphofructokinase‐1 (PFK1). Findings demonstrate that PPh could be used as a potential food source to reduce diabetic complications by regulating gene expression of antioxidant and glycolytic enzymes.

Consumption of underutilised grain legumes and the prevention of type II diabetes and cardiometabolic diseases: Evidence from field investigation and physicochemical analyses

This study was carried out to correlate grain legume consumption to the prevention of type II diabetes and some cardiometabolic diseases (CMD) (high blood pressure, obesity, and stroke). An exploratory survey was carried out among the population (n = 468) of the Diamaré division (Far-north, Cameroon). In addition, nutritional properties of selected grain legumes (GLs) were determined. Results showed generally that consumption of soybean, Bambara bean, and cowpea was linked to the prevention of metabolic diseases within the studied population. The nutritional properties of these GLs were also noteworthy. Remarkable protein content was noted in soybean's whole flour (WF) (38.133±0.366 g/100g DM), followed by the underutilised cultivar BVB of Bambara bean (26.434±0.366 g/100g DM). The cowpea seed has the highest total carbohydrate and vitamin C content of 59.294±0.129 g/100g DM and 327.715±0.336 µg EAA/100g DM, respectively, followed by the underutilised cultivar BVB with values of 57.696±0.097 g/100g DM and 261.951±0.376 µg EAA/100g DM. Dietary fibre content of Bambara bean seeds (18 - 28%) was higher than those of the other seeds, and probably plays important role in the prevention ability of diabetes and CMD of Bambara bean. Soybean's WF and those of the three underutilised Bambara bean cultivars contained the highest levels of total phenolic compounds and flavonoids, i.e., 206.089±0.087 mg GAE/100 DM, 143.868±0.299 mg QE/100g DM for soybean, respectively. The highest free radical scavenging activity (DPPH) was noted with the polyphenolic compounds’ extracts from soybean's WF, i.e., 21.193±0.049 µg TE/100g DM, followed by those from the underutilised BVB cultivar with a value of 16.594±0.160 µg TE/100g DM. The highest ferric reducing antioxidant power (FRAP) was obtained with soybean (34.481±0.029 µg TE/100g DM), followed by the cultivar GHB (32.036±0.076 µg TE/100g DM). The significant levels of protein, phenolic compounds, and dietary fibre in these seeds confirmed these correlations and their potential therapeutic effects and nutritional properties. Given the richness of the grain legumes in proteins and other bioactive compounds, raw materials and/or protein hydrolysates (peptides) will surely be a promising raw material for the pharmaceutical industries in the fight and/or prevention of metabolic diseases, in the fight against food insecurity, in the prevention and/or reversal of neurodegenerative diseases, and the formulation of a new functional ingredient.

Production of Bioactive Peptides from Baltic Herring (Clupea harengus membras): Dipeptidyl Peptidase-4 Inhibitory, Antioxidant and Antiproliferative Properties.

This study aimed to produce bioactive protein hydrolysates from undervalued fish, namely Baltic herring, and its filleting by-products. Protein hydrolysates were produced with Alcalase and Flavourzyme to achieve effective hydrolysis. The hydrolysates were evaluated for chemical composition, molecular weight distribution, antioxidant capacity, dipeptidyl-peptidase 4 (DPP4) inhibitory activity, effects on cell proliferation and surface hydrophobicity. The protein content of the hydrolysates was high, from 86% to 91% (dm), while the fat content was low, from 0.3% to 0.4% (dm). The hydrolysates showed high DPP4 inhibition activities with IC50 values from 5.38 mg/mL to 7.92 mg/mL. The scavenging activity of the hydrolysates towards DPPH was low, but an intermediate Folin–Ciocalteu reducing capacity and Cu2+ chelating ability was observed. The solid phase extraction with Sep-Pak C18 cartridges increased the DPP4 inhibition activity and antioxidant capacity, indicating peptides’ crucial role in the bioactivities. The cytotoxicity of the hydrolysates was evaluated on the HCT8, IMR90, and A549 cell lines. The hydrolysates inhibited cell growth in the cancer and normal cells, although they did not reduce cell viability and were not lethal. Overall, our results indicate that protein hydrolysates from Baltic herring have potential as health-promoting foods and nutraceuticals, especially for enhancing healthy blood glucose regulation.

Hazelnut peptide fractions preserve their bioactivities beyond industrial manufacture and simulated digestion of hazelnut cocoa cream

Cold press hazelnut cakes represent a concentrated source of proteins that can be industrially exploited. Previously, bioactive attributes of hazelnut protein hydrolysates including antihypertensive and antidiabetic activities were documented. Here, we made an attempt to utilize bioactive hazelnut protein hydrolysates (1 % w/w) in the manufacture of industrial hazelnut cocoa cream and investigate their stability through processing and simulated gastrointestinal digestion. The inclusion of bioactive peptide fractions was a safe practice in the microbiological sense. Proteolysis lowered the potential allergenicity of hazelnut proteins in the cocoa cream products up to about 20 %. In silico trypsinolysis predicted partial degradation for 51.8 % of the peptide sequences (i.e., 43/83) that were present in the hydrolysates. However, partial degradation and mixing of degraded vs non-degraded peptides preserved and/or further elevated bioactive attributes in the digested cocoa cream products in terms of Angiotensin converting enzyme (ACE)-inhibitory (up to about 92 %) and antidiabetic activities (between 7.5 and 44.4 %). In most cases, however, antioxidative activity was < 10 %. While simulated in vitro digestion potentially influenced the bioactive attributes of protein hydrolysates, the influence of cocoa cream processing and food matrix were relatively limited for hydrolysate fractions and more pronounced for protein isolates. Hazelnut press cakes represent a significant resource for the generation and industrial utilization of bioactive peptides, which could preserve their bioactivity beyond industrial manufacture and digestion and lead to slightly reduced allergenicity.

Encapsulation of Spirulina protein hydrolysates in liposomes: Impact on antioxidant activity and gastrointestinal behavior

A Spirulina hydrolysate was encapsulated within anionic liposomes composed of soybean lecithin and γ-oryzanol at an encapsulation efficiency of 90 %. A combination of 10 mg/mL hydrolysate and 1.3 mg/mL γ-oryzanol exhibited a significant synergism in inhibition of the formation of thiobarbituric acid-reactive substances (TBARS) and provided good protection of the liposomes against oxidation. The particle size of the liposomes increased significantly in the presence of the hydrolysate. Chitosomes were formed by coating the anionic liposomes with cationic chitosan. The antioxidant activity of the hydrolysate-loaded liposomes and chitosomes and free hydrolysate decreased under the highly acidic conditions in the stomach with the reduction in activity being greatest for the free hydrolysate. However, after exposure to small intestine conditions, the antioxidant activity of all formulations increased significantly (p < 0.05). This study highlights the potential of non-coated and coated liposomes to increase the stability and bioactivity of bioactive protein hydrolysates.

Bioactive Peptides: From Basic Research to Clinical Trials and Commercialization.

Chronic diseases, including metabolic diseases, have become a worldwide public health issue. Research regarding the use of bioactive peptides or protein hydrolysates derived from food, as the diet-based strategies for the prevention and mitigation of chronic diseases, has increased exponentially in the past decades. Numerous in vitro and in vivo studies report the efficacy and safety of food-derived bioactive peptides and protein hydrolysates as antihypertensive, anti-inflammatory, antidiabetic, and antioxidant agents. However, despite promising preclinical results, an inadequate understanding of their mechanisms of action and pharmacokinetics restrict their clinical translation. Commercialization of bioactive peptides can be further hindered due to scarce information regarding their efficacy, safety, bitter taste, as well as the lack of a cost-effective method of production. This review provides an overview of the current clinical evidence and challenges to commercial applications of food-derived bioactive peptides and protein hydrolysates for the prevention and alleviation of chronic diseases.