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Fish discards and by-products can be transformed into high value-added products such as fish protein hydrolysates (FPH) containing bioactive peptides. Protein hydrolysates were prepared from different parts (whole fish, skin and head) of several discarded species of the North-West Spain fishing fleet using Alcalase. All hydrolysates had moisture and ash contents lower than 10% and 15%, respectively. The fat content of FPH varied between 1.5% and 9.4% and had high protein content (69.8–76.6%). The amino acids profiles of FPH are quite similar and the most abundant amino acids were glutamic and aspartic acids. All FPH exhibited antioxidant activity and those obtained from Atlantic horse mackerel heads presented the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, reducing power and Cu2+ chelating activity. On the other hand, hydrolysates from gurnard heads showed the highest ABTS radical scavenging activity and Fe2+ chelating activity. In what concerns the α-amylase inhibitory activity, the IC50 values recorded for FPH ranged between 5.70 and 84.37 mg/mL for blue whiting heads and whole Atlantic horse mackerel, respectively. α-Glucosidase inhibitory activity of FPH was relatively low but all FPH had high Angiotensin Converting Enzyme (ACE) inhibitory activity. Considering the biological activities, these FPH are potential natural additives for functional foods or nutraceuticals.

The objective of this report was to investigate the isolation and recovery of different biocompounds and bioproducts from wastes (skins and heads) that were obtained from five species discarded by fishing fleets (megrim, hake, boarfish, grenadier, and Atlantic horse mackerel). Based on chemical treatments, enzymatic hydrolysis, and bacterial fermentation, we have isolated and produced gelatinous solutions, oils that are rich in omega-3, fish protein hydrolysates (FPHs) with antioxidant and antihypertensive activities, and peptones. FPHs showed degrees of hydrolysis higher than 13%, with soluble protein concentrations greater than 27 g/L and in vitro digestibilities superior to 90%. Additionally, amino acids compositions were always valuable and bioactivities were, in some cases, remarkable. Peptones that were obtained from FPHs of skin and the heads were demonstrated to be a viable alternative to expensive commercial ones indicated for the production of biomass, lactic acid, and pediocin SA-1 from Pediococcus acidilactici.

This study investigated the effect of heat treatment of edible insects on antioxidant and anti-inflammatory activities of peptides obtained by in vitro gastrointestinal digestion and absorption process thereof. The antioxidant potential of edible insect hydrolysates was determined as free radical-scavenging activity, ion chelating activity, and reducing power, whereas the anti-inflammatory activity was expressed as lipoxygenase and cyclooxygenase-2 inhibitory activity. The highest antiradical activity against DPPH• (2,2-diphenyl-1-picrylhydrazyl radical) was noted for a peptide fraction from baked cricket Gryllodes sigillatus hydrolysate (IC50 value 10.9 µg/mL) and that against ABTS•+ (2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical) was the highest for raw mealworm Tenebrio molitor hydrolysate (inhibitory concentration (IC50 value) 5.3 µg/mL). The peptides obtained from boiled locust Schistocerca gregaria hydrolysate showed the highest Fe2+ chelation ability (IC50 value 2.57 µg/mL); furthermore, the highest reducing power was observed for raw G. sigillatus hydrolysate (0.771). The peptide fraction from a protein preparation from the locust S. gregaria exhibited the most significant lipoxygenase and cyclooxygenase-2 inhibitory activity (IC50 value 3.13 µg/mL and 5.05 µg/mL, respectively).

Microalgae have been described as a source of bioactive compounds, such as peptides. Microalgae are easy to produce, making them a sustainable resource for extracting active ingredients for industrial applications. Several microalgae species have interesting protein content, such as Chlorella vulgaris with around 52.2% of protein, making it promising for peptide hydrolysate production. Therefore, this work focused on the production of water-soluble hydrolysates rich in proteins/peptides from the microalgae C. vulgaris and studied bioactive properties. For that, a design of experiments (DOE) was performed to establish the optimal conditions to produce hydrolysates with higher levels of protein, as well as antioxidant and antihypertensive properties. Four experimental factors were considered (cellulase percentage, protease percentage, hydrolysis temperature, and hydrolysis duration) for three responses (protein content, antioxidant activity, and antihypertensive activity). The optimal conditions determined by the DOE allowed producing a scaled-up hydrolysate with 45% protein, with antioxidant activity, measured by oxygen radical absorbance capacity assay, of 1035 µmol TE/g protein, IC50 for angiotensin-converting enzyme inhibition activity of 286 µg protein/mL, and α-glucosidase inhibition of 31% (30 mg hydrolysate/mL). The obtained hydrolysates can be used as functional ingredients for food and nutraceuticals due to their antioxidant, antihypertensive, and antidiabetic potential. Moreover, the antioxidant potential of the extracts may be relevant for the cosmetic industry, especially in antiaging formulations.

A new preservation approach is presented in this article to prolong the lifetime of raw chicken meat and enhance its quality at 4 °C via coating with highly soluble kidney bean protein hydrolysate. The hydrolysates of the black, red, and white kidney protein (BKH, RKH, and WKH) were obtained after 30 min enzymatic hydrolysis with Alcalase (E/S ratio of 1:100, hydrolysis degree 25–29%). The different phaseolin subunits (8S) appeared in SDS-PAGE in 35–45 kD molecular weight range while vicilin appeared in the molecular weight range of 55–75 kD. The kidney bean protein hydrolysates have considerable antioxidant activity as evidenced by the DPPH-scavenging activity and β-carotine-linolenic assay, as well as antimicrobial activity evaluated by disc diffusion assay. BKH followed by RKH (800 µg/mL) significantly (p ≤ 0.05) scavenged 95, 91% of DPPH and inhibited 82–88% of linoleic oxidation. The three studied hydrolysates significantly inhibited the growth of bacteria, yeast, and fungi, where BKH was the most performing. Kidney bean protein hydrolysates could shield the chicken meat because of their amphoteric nature and many functional properties (water and oil-absorbing capacity and foaming stability). The quality of chicken meat was assessed by tracing the fluctuations in the chemical parameters (pH, met-myoglobin, lipid oxidation, and TVBN), bacterial load (total bacterial count, and psychrophilic count), color parameters and sensorial traits during cold preservation (4 °C). The hydrolysates (800 µg/g) significantly p ≤ 0.05 reduced the increment in meat pH and TVBN values, inhibited 59–70% of lipid oxidation as compared to control during 30 days of cold storage via eliminating 50% of bacterial load and maintained secured storage for 30 days. RKH and WKH significantly (p ≤ 0.05) enhanced L*, a* values, thus augmented the meat whiteness and redness, while, BKH increased b* values, declining all color parameters during meat storage. RKH and WKH (800 µg/g) (p ≤ 0.05) maintained 50–71% and 69–75% of meat color and odor, respectively, increased the meat juiciness after 30 days of cold storage. BKH, RKH and WKH can be safely incorporated into novel foods.

A low-value by-product of cold-pressed sesame oil is defatted black sesame cake (DBSC). The remaining protein and essential amino acids may be utilized as a renewable biological source to produce bioactive products. The bioactivities of the protein hydrolysate from black sesame cake and its peptide fractions were examined in this study for in vitro antioxidant activity and inhibition of DPP-IV, ACE, α-amylase, α-glucosidase, and pancreatic lipase. By using Flavourzyme to hydrolyze DBSC, followed by ultrafiltration, fractions with peptide sizes of <3, 3–10, and >10 kDa were obtained. According to the findings, the products of DBSC could neutralize free radicals and prevent ferric ion redox reactions. The highest inhibitory effects were shown with low Mw peptides (<3 kDa) against ACE, DPP-IV, α-amylase, and α-glucosidase. DBSC has demonstrated potential as a nutraceutical or functional ingredient for preventing and treating disorders associated with free radicals, such as diabetes, hypertension, and hyperglycemia.

Food-derived antioxidant peptides can be explored as natural antioxidants due to their potential health benefits. In this study, antioxidant peptides were isolated and purified from pea protein hydrolysates (PPH). The DPPH and ABTS radical scavenging activities were used as indexes to purify the antioxidant peptides by a series of purification steps including ultrafiltration, ion exchange chromatography, G25 gel filtration chromatography, and reversed-phase chromatography. Three novel antioxidant peptides YLVN, EEHLCFR and TFY were identified, which all exhibited strong antioxidant activity in vitro. EEHLCFR showed stronger DPPH scavenging activity with an IC50 value of 0.027 mg/mL. YLVN showed stronger ABTS scavenging activity with an IC50 value of 0.002 mg/mL and higher ORAC values of 1.120 ± 0.231 μmol TE/μmol, which is even better than that of GSH. Three novel antioxidant peptides significantly elevated LO2 cells viability even at the concentration of 0.025 mg/mL, and cell viability enhanced to 53.42 ± 1.19%, 55.78 ± 1.03%, and 51.09 ± 1.06% respectively, compared to that of H2O2 injury group (48.35 ± 0.96%), and prevented the accumulation of ROS by enhancing the activities of antioxidant enzymes in H2O2-induced oxidative stress LO2 cells. The molecular docking results showed that the potential molecular mechanism of the three novel antioxidant peptides may be in high correlation with the activation of the Keap1-Nrf2 pathway by occupying the Keap1-Nrf2 binding site. These results demonstrate that the three novel antioxidant peptides are potential natural antioxidants that can be devoted to medicine or functional food ingredients.

Stone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including Ala-Leu-Gly-Pro-Gln-Phe-Tyr (794.44 Da), Lys-Val-Pro-Pro-Lys-Ala (638.88 Da), Leu-Ala-Pro-Pro-Thr-Met (628.85 Da), Glu-Val-Leu-Ile-Gln (600.77 Da) and Glu-His-Pro-Val-Leu (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.310 mM, 1.440 mM and 1.680 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.

In this research, sesame meal protein hydrolysate (SPH) was obtained from the sesame protein after hydrolysis by Bacillus coagulans . At first, the peptide concentration test was performed at different times to confirm the protease activity of B. coagulans . The chemical composition and total amino acid contents of sesame meal were determined. Fermentation conditions were optimized using response surface methodology (RSM). The results showed DPPH radical scavenging up to 70%, reducing power up to 0.779, and inhibitory activity against Staphylococcus aureus up to 78%, Escherichia coli up to 60%, Listeria monocytogenes up to 80% and Clostridium perfringens up to 85%. The antioxidant activity of the optimal sample was investigated at concentrations ranging from 10 to 50 mg/mL. The results demonstrated that 50 mg/mL of the SPH had the highest antioxidant activity. Analysis of amino acids by HPLC revealed that glutamic acid and glycine had the highest concentrations, and all essential amino acids were detected. SEM analysis showed smaller heterogeneous particles of protein hydrolysate, which confirmed the hydrolysis process during fermentation. FTIR results showed that different functional groups were formed, which confirmed the hydrolysis of sesame protein. Generally, sesame protein can be a good source in the fermentation system by B. coagulans to produce hydrolysate with antimicrobial and antioxidant properties.

Diabetic nephropathy (DN) poses a significant health challenge, necessitating novel therapeutic approaches. In this study, we isolated proteins from cell-free supernatant (CFS) from the culture of the lactic acid bacteria Lactobacillus brevis RAMULAB49 strain. The proteins were subjected to simulated in vitro gastrointestinal digestion using gut enzymes – pepsin, pancreatin, and trypsin. The hydrolysates were filtered using 3kDa threshold ultra-centrifugal filters and were desalted using C18 disks. This was followed by nLC-ESI MS/MS tandem mass spectrometry-based identification of peptides, leading in the identification of a of 258 unique peptides across three enzyme combinations. The resultant sequences were made into peptide library construction based on their, bioactivity scores, allergenicity, toxicity, and antidiabetic potential, a total of 10 peptides was constructed and modeled in 3D. On the other hand, 266 DN associated genes were identified using a network pharmacology approach. The resultant protein-protein (PPI) network was analysed using the gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment approaches, resulting in identification of critical pathways, ERK1, PI3K-Akt, EGRF and TNF signaling as significantly involved in DN, where, ERK1 emerging as a key node due to its involvement in cell proliferation, inflammation, and fibrosis associated with DN. Top two 3D-modelled bioactive peptides were selected for interaction study with the target protein ERK1. Peptide TNEDPYTIDVES showed a strong binding energy of −9.9 kcal/mol, at the ATP-binding site and dynamics simulations confirmed the structural stability of this complex over 100 ns, showing consistent hydrogen bond interactions and RMSD values below 2.5 Å. These findings suggest that TNEDPYTIDVES may act as a competitive ERK1 inhibitor by occupying the adenine-mimicking ATP-binding cleft, thereby interfering with phosphorylation activity. This integrative approach highlights L. brevis RAMULAB49 strain derived peptides as promising candidates for the development of peptide-based therapeutics target and could pave the way for new drug development treating diabetic nephropathy.