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Ribosomally synthesized and post-translationally modified peptides (RiPPs) represent a significant potential for novel therapeutic applications because of their bioactive properties, stability, and specificity. RiPPs are synthesized on ribosomes, followed by intricate post-translational modifications (PTMs), crucial for their diverse structures and functions. PTMs, such as cyclization, methylation, and proteolysis, play crucial roles in enhancing RiPP stability and bioactivity. Advances in synthetic biology and bioinformatics have significantly advanced the field, introducing new methods for RiPP production and engineering. These methods encompass strategies for heterologous expression, genetic refactoring, and exploiting the substrate tolerance of tailoring enzymes to create novel RiPP analogs with improved or entirely new functions. Furthermore, the introduction and implementation of cutting-edge screening methods, including mRNA display, surface display, and two-hybrid systems, have expedited the identification of RiPPs with significant pharmaceutical potential. This comprehensive review not only discusses the current advancements in RiPP research but also the promising opportunities that leveraging these bioactive peptides for therapeutic applications presents, illustrating the synergy between traditional biochemistry and contemporary synthetic biology and genetic engineering approaches.

Inflammation is a normal immune response in organisms, but it often triggers chronic diseases such as colitis and arthritis. Currently, the most widely used antiinflammatory drugs are non-steroidal anti-inflammatory drugs, albeit they are accompanied by various adverse effects such as hypertension and renal dysfunction. Bioactive peptides (BAPs) provide therapeutic benefits for inflammation and mitigate side effects. Herein, this review focuses on the therapeutic effects of various BAPs on inflammation in different body parts. Emphasis is placed on the immunomodulatory mechanisms of BAPs in treating inflammation, such as regulating the release of inflammatory mediators, modulating MAPK and NF-κB signaling pathways, and reducing oxidative stress reactions for immunomodulation. This review aims to provide a reference for the function, application, and anti-inflammation mechanisms of BAPs. [ABSTRACT FROM AUTHOR]

With hyperlipidemia posing a significant cardiovascular risk, innovative strategies are essential to unlock new therapeutic possibilities. Probiotic fermentation of milk proteins offers a natural and effective means to produce peptides with hypolipidemic properties, providing a promising approach to lowering lipid levels and reducing cardiovascular risk. In this study, fermented cattle milk (FCTM), fermented camel milk (FCM), fermented goat milk (FGM), and fermented sheep milk (FSM) were produced using a total of five probiotic bacterial strains to investigate the release of bioactive peptides (BAPs) with hypolipidemic potential via in vitro inhibitory activity toward pancreatic lipase (PL) during a 14-day refrigerated storage study. The PL inhibitory activities of these fermented milk (FM) varied according to the types of probiotic strains and milk types used. Overall, the Pediococcus pentosaceus MF000957 (PP-957) strain showed the highest PL inhibitory activity spanning across all milk types, and therefore, PP-957-derived fermented samples were analyzed for BAP identification by LCMS-QTOF. The identified BAPs were further analyzed using in silico and bioinformatics approaches for bioactivity prediction, molecular docking, and drug pharmacokinetic studies. Overall, four peptides derived from FCTM, one from FCM, and two peptides common in FGM and FSM were predicted as active PL inhibitors based on their binding energy and number of binding sites on the PL enzyme. All peptides were non-toxic, non-carcinogenic, and had appropriate drug-like properties. The outcomes of this study suggest that FM-derived peptides from animal milk are anticipated to be useful for combating hypercholesterolemia. [ABSTRACT FROM AUTHOR]

This study investigates the production of protein hydrolysates with dipeptidyl peptidase-IV (DPP-IV) inhibitory activity from agro-industrial by-products, namely olive seed, sunflower seed, rapeseed, and lupin meals, as well as from two plant protein isolates such as pea and potato. Furthermore, the effect of simulated gastrointestinal digestion on the DPP-IV inhibitory activity of all the hydrolysates was evaluated. Overall, the lowest values of IC50 (1.02 ± 0.09–1.24 ± 0.19 mg protein/mL) were observed for the hydrolysates with a high proportion of short-chain [<1 kDa] peptides (i.e., olive seed, sunflower seed, and lupin) or high content of proline (i.e., rapeseed). Contrarily, the IC50 of the pea and potato hydrolysates was significantly higher (1.50 ± 0.13–1.93 ± 0.13 mg protein/mL). In vitro digestion led to an increase in peptides < 1 kDa for almost all hydrolysates (except olive and sunflower seed meals), which was noticeable for rapeseed, pea, and potato hydrolysates. Digestion did not significantly modify the DPP-IV inhibitory activity of olive, sunflower, rapeseed, and potato hydrolysates, whereas a significant decrease in IC50 value was obtained for pea hydrolysate and a significant increase in IC50 was obtained for lupin hydrolysate. Thus, this work shows the potential of agro-industrial by-products for the production of protein hydrolysates exhibiting DPP-IV inhibition. [ABSTRACT FROM AUTHOR]

Soy sauce cake (SSC) is a by-product of soy sauce production. SSC often goes underutilized due to its high salt content. To address this, halophilic bacterium was employed for SSC fermentation, aiming to release bioactive peptides in addition to the waste management advantages. Using a bioinformatics approach, in silico proteolysis of soy glycinin which was simulated with six selected proteases mined from the genomes of Virgibacillus spp. yielded 29 non-toxic antioxidant peptides, mainly two to three amino acids in size (250–360 Da). Approximately 59% of these peptides had acidic isoelectric points, negative net charges, and moderate Boman index values. Peptides HL, LW, and TY were predicted as non-allergens with positive human intestinal absorption. Furthermore, submerged fermentation of SSC by Virgibacillus sp. strain CD6 under optimal conditions (2.5% inoculum, 72-h fermentation) produced a hydrolysate with the highest peptide content (2.4 mg/g). This hydrolysate demonstrated potential ferric reducing antioxidant power (FRAP) (57%) and 1,1-diphenyl-2-picryl hydrazine (DPPH) radical scavenging activity (31%). This study pioneers the use of in silico methods and submerged fermentation with halophilic bacterium to enhance the value of high-salt SSC by releasing antioxidant peptides. It addresses waste disposal challenges and reveals new opportunities for SSC in food product development. [ABSTRACT FROM AUTHOR]

The skin of amphibians is a rich source of peptides with a wide range of biological activities. They are stored in secretory granules in an inactive form. Upon stimulation, they are secreted together with proteases into the skin. Once activated, they rapidly exert their biological effects, including fighting microorganisms and predators, while their excess is immediately destroyed by the released proteases. To keep bioactive peptides in their initial form, it is necessary to inhibit these enzymes. Several inhibitors for this purpose have previously been mentioned; however, there has not been any reliable comparison of their efficiency so far. Here, we studied the efficiency of methanol and hydrochloric and formic acids, as well as phenylmethylsulfonyl fluoride, in the inhibition of nine frog peptides with the known sequence, belonging to five families in the secretion of Pelophylax esculentus. The results demonstrated that methanol had the highest inhibitory efficiency, while phenylmethylsulfonyl fluoride was the least efficient, probably due to its instability in aqueous media. Possible cleavages between certain amino acid residues in the sequence were established for each of the inhibitors. These results may be helpful for future studies on the nature of proteases and on prediction of the possible cleavage sites in novel peptides. [ABSTRACT FROM AUTHOR]

Integrated bioinformatics tools have created more efficient and robust methods to overcome in vitro challenges and have been widely utilized for the investigation of food proteins and the generation of peptide sequences. This study aimed to analyze the physicochemical properties and bioactivities of novel peptides derived from hydrolyzed milkfish (Chanos chanos) protein sequences and to discover their potential angiotensin-converting enzyme (ACE)- and dipeptidyl peptidase-4 (DPPIV)-inhibitory activities using machine learning-based tools, including BIOPEP-UWM, PeptideRanker, and the molecular docking software HADDOCK 2.4. Nine and three peptides were predicted to have ACE- and DPPIV-inhibitory activities, respectively. The DPPIV-inhibitory peptides were predicted to inhibit the compound with no known specific mode. Meanwhile, two tetrapeptides (MVWH and PPPS) were predicted to possess a competitive mode of ACE inhibition by directly binding to the tetra-coordinated Zn ion. Among all nine discovered ACE-inhibitory peptides, only the PPPS peptide satisfied the drug-likeness analysis requirements with no violations of the Lipinski rule of five and should be further investigated in vitro. [ABSTRACT FROM AUTHOR]

This study investigated the antioxidant and antidiabetic properties of soursop (Annona muricata) leaf biomass hydrolysates (SLH) extracted from the leaf proteins. The results revealed that flavourzyme-generated SLH showed the highest peptide content when compared to alcalase- and trypsin-generated SLH. Application of response surface methodology (RSM) remarkably increased peptide content under the optimized conditions at an E/S ratio of 4% (w/w), hydrolysis time of 4 h, a temperature of 50 °C, and pH of 7. SLH demonstrated stronger antioxidant (DPPH (22.92%) and ABTS (90.55%)) and antidiabetic (α-glucosidase inhibition (66.44%) and α-amylase inhibition (58.50%)) activities. A total of 14 peptides were identified as bioactive peptides, among which two peptides (FLAISPKAMK and WDSKWTHI) possessed the highest binding probability toward α-glucosidase and α-amylase. These peptides contain hydrophobic amino acids, which are important in improving the antioxidant activities of peptides. In conclusion, SLH could be useful for diabetes prevention. [ABSTRACT FROM AUTHOR]

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Sweet whey (SW) and yogurt acid whey (YAW) are dairy by-products of the cheese-making process and Greek-style yogurt production, respectively. Both of them are considered pollutants with huge volumes of SW and YAW produced due to the growing demand for dairy products worldwide. Moreover, whey-derived peptides, resulting from fermentation as well as from further hydrolysis during digestion, have been associated with various biological activities. In the present study, the angiotensin-converting enzyme (ACE)-inhibitory activity of 48 SW samples and 33 YAW samples from bovine, ovine, caprine, and ovine/caprine milk obtained were evaluated. Additionally, the SW and YAW digestates and two of their fractions (smaller than 10 kDa, SW-D-P10 and YAW-D-P10, and smaller than 3 kDa, SW-D-P3 and YAW-D-P3), which were obtained after in vitro digestion and subsequent ultrafiltration, were also subjected to evaluation. Our data indicated that the D-P10 and D-P3 fractions exhibited higher ACE-inhibitory activity compared to the corresponding values before digestion. The ACE-inhibitory capacity after in vitro digestion was higher for the ovine SW samples compared to their bovine and caprine counterparts. The effect of the D-P3 fraction on the inhibition of nitric oxide (NO) production and the expression of a selected panel of immune-response-related genes in LPS-stimulated RAW 264.7 macrophages was also evaluated. Fractions from both dairy by-products inhibited NO production in LPS-stimulated RAW 264.7 cells. Especially, ovine SW-D-P3 showed a strong NO inhibitory activity and suppressed inducible nitric oxide synthase (Nos2) mRNA levels. However, YAW-D-P3 could not trigger neither the gene expression of inflammatory macrophage mediators Nos2 and cyclooxygenase-2 (Ptgs2) nor tumor necrosis factor-α (Tnf) and interleukin 6 (Il6) in LPS-stimulated murine macrophages regardless of animal origin. These findings suggest that in vitro digestion could enhance the production of ACE-inhibitory peptides in both dairy by-products, while SW from ovine origin displays higher potential as an anti-inflammatory agent, effectively preventing excessive NO production. [ABSTRACT FROM AUTHOR]

Resource-intensive processes currently hamper the discovery of bioactive peptides (BAPs) from food by-products. To streamline this process, in silico approaches present a promising alternative. This study presents a novel computational workflow to predict peptide release, bioactivity, and bioavailability, significantly accelerating BAP discovery. The computational flowchart has been designed to identify and optimize critical enzymes involved in protein hydrolysis but also incorporates multi-enzyme screening. This feature is crucial for identifying the most effective enzyme combinations that yield the highest abundance of BAPs across different bioactive classes (anticancer, antidiabetic, antihypertensive, anti-inflammatory, and antimicrobial). Our process can be modulated to extract diverse BAP types efficiently from the same source. Here, we show the potentiality of our method for the identification of diverse types of BAPs from by-products generated from Solanum lycopersicum, the widely cultivated tomato plant, whose industrial processing generates a huge amount of waste, especially tomato peel. In particular, we optimized tomato by-products for bioactive peptide production by selecting cultivars like Line27859 and integrating large-scale gene expression. By integrating these advanced methods, we can maximize the value of by-products, contributing to a more circular and eco-friendly production process while advancing the development of valuable bioactive compounds. [ABSTRACT FROM AUTHOR]

Summary: The objectives of this study were to analyse the impact of both temperature and different isolates on microbial protease production ability and to examine the hypertensive effect of bioactive peptides (BAPs) that inhibit the angiotensin I‐converting enzyme released by fermentation of non‐fat milk. First, the ability of several Yamadazyma spp. isolates, which were previously isolated and identified from several sources, was screened in terms of the production of proteolytic enzymes at 15 and 25 °C. The effect of temperature on proteolysis activity of selected isolates was considerable, and incubation at 25 °C was favourable for protease production. Besides, combinations of three different isolates showed remarkable proteolytic activity during the incubation periods of 24, 48 and 72 h. The highest angiotensin I‐converting enzyme inhibitory (ACE‐I) activity was detected for the combination Yamadazyma spp. BO10 and B514‐1, with an inhibition of 92.5%. The partial purification of peptides by ultrafiltration (cut‐off 10 kDa) has no crucial impact on ACE‐I activity, and further purification might improve their effectiveness. The implications of fermentation with co‐culture may have symbiotic potential to increase the antihypertensive effect of the product. Therefore, these results suggest that Yamadazyma spp. may be used to produce functional products or bioactive peptides presenting health‐promoting attributes. [ABSTRACT FROM AUTHOR]

Plant protein components contribute positively to human well-being as they modulate the immune status of a consumer, especially when the enzymatic method is employed in order to release their bioactive peptides. These peptides are derived from plant-based foods such as soy, wheat, barley, rye, oats, rice, corn, sorghum, and millet, the famous staple foods around the world. Since these peptides are crucial to functional food among other key industries, the present study endeavored to scout for relevant information within the past three decades, using the Web of Science, Scopus, and Google search engines. In this review, first, the core of immunomodulation and types of immunomodulatory agents will be discussed, followed by the production of plant-based immunomodulatory peptides and their immunomodulatory mechanisms in cells, animals, and humans are also studied. Finally, applications and challenges associated with plant-based immunomodulatory peptides are put forward. [ABSTRACT FROM AUTHOR]

Cardiovascular diseases (CVDs) affect the quality of life or are fatal in the worst cases, resulting in a significant economic and social burden. Therefore, there is an urgent need to invent functional products or drugs for improving patient health and alleviating and controlling these diseases. Marine bioactive peptides reduce and control CVDs. Many of the predisposing factors triggering CVDs can be alleviated by consuming functional foods containing marine biopeptides. Therefore, improving CVD incidence through the use of effective biopeptide foods from marine sources has attracted increasing interest and attention. This review reports information on bioactive peptides derived from various marine organisms, focusing on the process of the separation, purification, and identification of biological peptides, biological characteristics, and functional food for promoting cardiovascular health. Increasing evidence shows that the bioactivity and safety of marine peptides significantly impact their storage, purification, and processing. It is feasible to develop further strategies involving functional foods to treat CVDs through effective safety testing methods. Future work should focus on producing high‐quality marine peptides and applying them in the food and drug industry. [ABSTRACT FROM AUTHOR]

Lactobacillus acidophilus is a probiotic bacterium that possesses numerous health-promoting properties and has significant technological applications in the fermentation of a wide range of food products and beverages. This review discusses the health benefits of L. acidophilus, including its ability to enhance immunity; promote digestive wellness; and exhibit antioxidant, antitumor, and antimicrobial properties. This review also discusses the production of bioactive peptides and extracellular polysaccharides (EPS) by L. acidophilus. Factors, such as salinity, temperature, carbon sources, and nutrient availability, influence the growth of L. acidophilus, which can affect the survival and bioactive potential of fermented products. The proteolytic effects of L. acidophilus contribute to protein breakdown, which leads to the release of bioactive peptides with various health benefits. This review also discusses the applications of L. acidophilus in the fermentation of dairy products, cereal beverages, soymilk, fruit and vegetable juices, and other functional food preparations, highlighting its potential for improving the nutritional value, organoleptic properties, and probiotic delivery of these products. This review highlights the importance of understanding and controlling fermentation conditions to maximize the growth and health-promoting benefits of L. acidophilus in various food and beverage products. [ABSTRACT FROM AUTHOR]

Brewers' spent grain (BSG), the major brewing by-product, is a rich source of proteins. However, the color and low solubility of BSG proteins (BSGP) are two main challenges that have restricted its application in food formulations. The objective of this study was to overcome these challenges via enzymatic hydrolysis of BSGP. In this approach, proteases from several origins were used, including Alcalase (bacterial), flavourzyme (fungal), papain (plant), and pancreatin (animal). Moreover, the evaluation of techno-functional and bioactive properties of BSGP hydrolysates was another part of this study. A response surface methodology (RSM) was applied for the optimization of BSGP extraction through the alkaline method. Extraction in optimized conditions, i.e., 2.12 h, 79.61 °C, and 67.52% H2O2, resulted in the highest extraction yield (28.18%) and lightness (66.89) which allowed a protein recovery of 64.53%. The highest solubility in neutral pH (47.56%) and water absorption capacity (3.87 (g/g)) were found for pancratin hydrolysate. The highest emulsion capacity was also related to pancratin hydrolysate, with emulsifying activity index = 84.98 (m2/g) and emulsifying stability index = 76.63%, respectively. The Alcalase hydrolysate showed the strongest scavenging activity against ABTS (IC50 = 1.7 ± 0.08 mg/mL) and DPPH radicals (IC50 = 2.47 ± 0.07 mg/mL), while flavourzyme hydrolysate had the best α-glucosidase inhibitory (IC50 = 9.25 mg/mL). This research presents BSG as a low-cost protein resource for the production of enzymatic protein hydrolysates with enhanced techno-functional and bioactive properties. [ABSTRACT FROM AUTHOR]

The emergence of resistant microorganisms has reduced the effectiveness of currently available antimicrobials, necessitating the development of new strategies. Plant antimicrobial peptides (AMPs) are promising candidates for novel drug development. In this study, we aimed to isolate, characterize, and evaluate the antimicrobial activities of AMPs isolated from Capsicum annuum. The antifungal potential was tested against Candida species. Three AMPs from C. annuum leaves were isolated and characterized: a protease inhibitor, a defensin-like protein, and a lipid transporter protein, respectively named CaCPin-II, CaCDef-like, and CaCLTP2. All three peptides had a molecular mass between 3.5 and 6.5 kDa and caused morphological and physiological changes in four different species of the genus Candida, such as pseudohyphae formation, cell swelling and agglutination, growth inhibition, reduced cell viability, oxidative stress, membrane permeabilization, and metacaspase activation. Except for CaCPin-II, the peptides showed low or no hemolytic activity at the concentrations used in the yeast assays. CaCPin-II inhibited α-amylase activity. Together, these results suggest that these peptides have the potential as antimicrobial agents against species of the genus Candida and can serve as scaffolds for the development of synthetic peptides for this purpose. [ABSTRACT FROM AUTHOR]

Healthy and sustainable diets have seen a surge in popularity in recent years, driven by a desire to consume foods that not only help health but also have a favorable influence on the environment, such as plant-based proteins. This has created controversy because plant-based proteins may not always contain all the amino acids required by the organism. However, protein extraction methods have been developed due to technological advancements to boost their nutritional worth. Furthermore, certain chemicals, such as bioactive peptides, have been identified and linked to favorable health effects. As a result, the current analysis focuses on the primary plant-based protein sources, their chemical composition, and the molecular mechanism activated by the amino acid types of present. It also discusses plant protein extraction techniques, bioactive substances derived from these sources, product development using plant protein, and the therapeutic benefits of these plant-based proteins in clinical research. [ABSTRACT FROM AUTHOR]

The interest in algae-derived bioactive compounds has grown due to their potential therapeutic efficacy against a range of diseases. These compounds, derived from proteins, exhibit diverse functions and profound pharmacological effects. Recent research has highlighted the extensive health benefits of algae-derived bioactive compounds, positioning them as potential natural antioxidants in the food, pharmaceutical, and cosmetic industries. This study focuses on extracting proteins from Porphyra yezoensis using innovative physical pre-treatment methods such as stirring, ball milling, and homogenization, under various acidic and alkaline conditions. Enzymatic hydrolysis, employing commercial enzymes at optimal temperature, pH, and enzyme–substrate ratios, produced distinct fractions according to molecular weight. Pepsin demonstrated the highest hydrolysis rate, with the fraction above 10 kDa identified as the most bioactive hydrolysate. Antioxidant activity was evaluated through DPPH, ABTS, ferrous ion chelation, and reducing power assays, demonstrating high antioxidant potential and the ability to mitigate oxidative stress. The 10 kDa fraction of pepsin hydrolysate exhibited 82.6% DPPH activity, 77.5% ABTS activity, 88.4% ferrous ion chelation activity, and higher reducing power potential (0.84 absorbance at 700 nm). Further exploration of mechanisms, amino acid profiles, and potential in vivo benefits is essential to fully exploit the medicinal potential of these algae-derived hydrolysates. [ABSTRACT FROM AUTHOR]

Prolyl oligopeptidase (POP) is a conserved serine protease belonging to proline-specific peptidases. It has both enzymatic and non-enzymatic activity and is involved in numerous biological processes in the human body, playing a role in e.g., cellular growth and differentiation, inflammation, as well as the development of some neurodegenerative and neuropsychiatric disorders. This article describes the physiological and pathological aspects of POP activity and the state-of-art of its peptidic inhibitors originating from food proteins, with a particular focus on their potential as cognition-enhancing agents. Although some milk, meat, fish, and plant protein-derived peptides have the potential to be applied as natural, procognitive nutraceuticals, their effectiveness requires further evaluation, especially in clinical trials. We demonstrated that the important features of the most promising POP-inhibiting peptides are very short sequence, high content of hydrophobic amino acids, and usually the presence of proline residue. [ABSTRACT FROM AUTHOR]

Chronic diseases have emerged as a formidable global health concern, with their prevalence steadily rising over the years. Several approaches to addressing these concerns include the use of medications, which are often expensive, contain synthetic chemical substances, and have reported adverse effects. The use of foods, especially proteins, as an alternative approach to addressing chronic health concerns by treating and managing chronic diseases is increasing. This review evaluates the intriguing role of food proteins in mitigating chronic diseases and improving our understanding of the therapeutic potential of different protein types, including those derived from legumes, nuts, and seeds, dairy, fish, and numerous other sources. They have been reported to offer promising avenues for managing chronic diseases, including cardiovascular diseases, diabetes, chronic inflammation, weight management, bone health, glycemic control, muscle preservation, and many other health benefits. Although the exact mechanisms for these actions are still not properly elucidated, it is, however, understood that food proteins exert these health-beneficial effects by their unique nutritional and bioactive profiles, especially their bioactive peptides and amino acids. Practical applications are also discussed, including dietary interventions that are tailored towards incorporating protein-rich foods and the development of functional foods for disease prevention and management. Food proteins are a promising approach to combating chronic diseases that can turn around public health practices. [ABSTRACT FROM AUTHOR]

Chicken meat production has increased over the years, leading to a proportional increase in waste generation, which often contains high levels of proteins, such as viscera. Therefore, this study aimed to investigate the enzymatic hydrolysis of chicken viscera proteins as a strategy to value solid waste from the poultry industry. The hydrolysates were characterized for their antioxidant properties and molecular weight distribution. Additionally, the enzymatic hydrolysis process was scaled up from 125 mL flasks with 50 mL of protein solution to 3 L using a 6 L bioreactor. The enzymatic hydrolysis of chicken viscera proteins using a binary mixture of proteases (85.25 U/mL of each enzyme, Alcalase and Flavourzyme, totaling 170.5 U/mL) resulted in an increase of up to 245% in 2,2-azinobis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging, 353% 2,2-diphenyl-1-picryl-hydrazyl (DPPH) in radical scavenging, 69% in Ferric Reducing Antioxidant Power Assay (FRAP) and 146% in total reducing capacity (TRC). The antioxidant properties of the protein hydrolysates are preserved during the scale-up of enzymatic hydrolysis. Protein fractions smaller than 5 kDa showed the highest ABTS and DPPH radical scavenging activities, while fractions greater than 30 kDa showed the best results for the FRAP method. [ABSTRACT FROM AUTHOR]

The Jatropha curcas cake, a protein-rich by-product of biofuel production, was the subject of our study. We identified and quantified the ACE inhibitory, antioxidant, and antidiabetic activities of bioactive peptides from a Jatropha curcas L. var Sevangel protein isolate. The protein isolate (20.44% recovered dry matter, 38.75% protein content, and 34.98% protein yield) was subjected to two enzyme systems for hydrolysis: alcalase (PEJA) and flavourzyme (PEJF), recording every 2 h until 8 h had passed. The highest proteolytic capacity in PEJA was reached at 2 h (4041.38 ± 50.89), while in PEJF, it was reached at 6 h (3435.16 ± 59.31). Gel electrophoresis of the PEJA and PEJF samples showed bands corresponding to peptides smaller than 10 kDa in both systems studied. The highest values for the antioxidant capacity (DPPH) were obtained at 4 h for PEJA (56.17 ± 1.14), while they were obtained at 6 h for PEJF (26.64 ± 0.52). The highest values for the antihypertensive capacity were recorded at 6 h (86.46 ± 1.85) in PEJF. The highest antidiabetic capacity obtained for PEJA and PEJF was observed at 6 h, 68.86 ± 8.27 and 52.75 ± 2.23, respectively. This is the first report of their antidiabetic activity. Notably, alcalase hydrolysate outperformed flavourzyme hydrolysate and the cereals reported in other studies, confirming its better multi-bioactivity. [ABSTRACT FROM AUTHOR]

Bioactive peptides derived from foods provide physiological health benefits beyond nutrition. This study focused on profiling small peptide inhibitors against two key serine proteases, dipeptidyl peptidase‐IV (DPP‐IV) and prolyl oligopeptidase (POP). DPP‐IV is a well‐known protein involved in diverse pathways regulating inflammation, renal, cardiovascular physiology, and glucose homeostasis. POP is yet another key target protein for neurodegenerative disorders. The study evaluated peptide libraries of buffalo colostrum whey and fat globule membrane proteins derived from pepsin and pepsin–pancreatin digestion through in silico web tools and structure‐based analysis by molecular docking and binding free‐energy estimation, followed by in vitro assay for DPP‐IV inhibition for the lead peptides. The bioinformatic study indicated 49 peptides presented motifs with DPP‐IV inhibition while 5 peptides with sequences for POP inhibition. In the molecular docking interactions study, 22 peptides interacted with active site residues of DPP‐IV and 3 peptides with that of POP. The synthesized peptides, SFVSEVPEL and LTFQHNF inhibited DPP‐IV in vitro with an IC50 of 193.5 μM and 1.782 mM, respectively. The study revealed the key residues for inhibition of DPP‐IV and POP thus affirming the DPP‐IV inhibitory potential of milk‐derived peptides. [ABSTRACT FROM AUTHOR]

The coronavirus 2 (SARS‐CoV‐2), a positive‐sense RNA virus that causes severe acute respiratory illness, is the cause of Coronavirus Disease 2019 (COVID‐19) and Monkeypox is a zoonotic viral disease caused by a double‐strand enveloped DNA virus, a member of the Poxviridae family under the umbrella of the Orthopoxvirus genus. These viruses have harmed global health, societal stability, and global economy prompting the development of new therapeutic options. The purpose of this study was to analyze the potency of hazelnut‐derived bioactive peptides for usage in preventive measures against SARS‐CoV‐2 and Monkeypox infections. Since SARS‐CoV‐2 entry into the host cell takes place through angiotensin‐converting enzyme (ACE) receptors, an in silico attempt was made here to analyze the previously characterized ACE‐inhibitory hazelnut peptides for their anti‐COVID potential. First of all, peptide sequences with PeptideRanker values >0.5 were determined, where 43 of 256 hazelnut peptides met this condition. BIOPEP tools were used to calculate their ACE‐inhibitory characteristics. VPHW and DENPRHF demonstrated the strongest ACE‐inhibitory activity based on BIOPEP analysis. The binding potentials of VPHW (p < 0.001) and DENPRHF (p < 0.001) peptides to ACE were statistically significant based on PepSite2 analysis. The hazelnut‐derived peptides were docked with ACE, spike proteins, SARS‐CoV‐2 proteases, host cell receptors, and Monkeypox 2022 membrane proteins using HPEPDOCK and CABS‐dock. The in silico findings pointed out potential inhibition of SARS‐CoV‐2 main protease in the host cell and Monkeypox 2022 membrane protein and demonstration of multiple bioactivities. [ABSTRACT FROM AUTHOR]

Sacha inchi (Plukenetia volubilis L.) is an under-exploited crop with great potential due to its nutritional and medicinal characteristics. A Sacha inchi protein isolate (SII), obtained from defatted Sacha inchi flour (SIF), was hydrolyzed by Bioprotease LA 660 under specific conditions. The hydrolysates were characterized chemically, and their digestibility and antioxidant capacity were evaluated by in vitro cell-free experiments to select the hydrolysate with major antioxidant activity. Sacha inchi protein hydrolysate at 20 min (SIH20B) was selected, and the anti-inflammatory capacity was evaluated by RT-qPCR and ELISA techniques, using two different doses in monocytes THP-1 stimulated with lipopolysaccharide (LPS). The results obtained showed that the in vitro administration of SIH20B down-regulated the TNF-α gene and reduced the release of this cytokine, whereas the anti-inflammatory cytokines IL-10 and IL-4 were up-regulated in LPS-stimulated monocytes and co-administrated with SIH20B. The peptides contained in SIH20B were identified, and the 20 more relatively abundant peptides with a mass by 1 kDa were subjected to in silico analysis to hypothesize those that could be responsible for the bioactivity reported in the hydrolysate. From the identified peptides, the peptides AAGALKKFL and LGVKFKGGL, among others, are proposed as the most biologically actives. In conclusion, SIH20B is a novel, natural source of high-value-added biopeptides that could be used as an ingredient in formulations of food or nutraceutical compounds. [ABSTRACT FROM AUTHOR]

This study explored the impact of starter-assisted fermentation on apple blossoms to enhance their potential as a source of antioxidant and antifungal molecules. Fructobacillus fructosus PL22 and Wickerhamomyces anomalus GY1 were chosen as starters owing to their origin and promising ability to modify plant secondary metabolites. An initial assessment through microbiological and physicochemical analyses showed superior outcomes for starter-assisted fermentation compared to the spontaneous process. Enzymatic hydrolysis of proteins, primarily controlled by starters, orchestrated the generation of new low-molecular-weight peptides. W. anomalus GY1 also induced modifications in the phenolic profile, generating a diverse array of bioactive metabolites. These metabolic changes, particularly the release of potentially bioactive peptides, were associated with significant antioxidant activity and marked antifungal efficacy against three common mold species. Our results shed light on the potential of microbial starters to valorize agricultural wastes and convert them into a valuable resource for industry. [ABSTRACT FROM AUTHOR]

Soft confections can serve as a reservoir for bioactive peptide delivery in both functional food and food supplement applications. In this study, pectin-based soft confections were fortified with proteolytic plant protein hydrolysates and the residual bioactivity of hydrolysates was studied after processing or simulated digestion. Cold press sunflower or hazelnut cakes were used in the manufacture of protein isolates based on an alkali extraction-isoelectric precipitation (AE-IP) method. Trypsin or bromelain were utilized in the proteolysis of the isolates and thus prepared liquid hydrolysates were used in confectionery manufacture. DPP-IV (dipeptidyl peptidase-IV) inhibitory activity (i.e., in vitro antidiabetic activity) and antioxidative activities were measured. In addition, sensory and textural attributes were investigated. In all cases, a significant concentration of hydrolysates were added to the confections (27%), which lead to significant changes in color, texture and sensory acceptance. The peptide profile and size distribution mostly altered such characteristics, while observed bioactivity was significant after processing. Simulated digestion enhanced DPP-IV inhibitory activity up to approx. 40%, whereas antioxidative performance decreased. While the applicability of the current findings is limited by hydrolysate solubility, ingredient interactions, and processing costs, the relevance of degree of hydrolysis (DH%), peptide characteristics and phenolic-peptide interactions on product quality and eventual bioactivity are being discussed. [ABSTRACT FROM AUTHOR]

For centuries, humans have used mushrooms as both food and pro-health supplements. Mushrooms, especially those related to the functions of the human immune system, are rich in dietary fiber, minerals, essential amino acids, and various bioactive compounds and have significant health-promoting properties. Immunoregulatory compounds in mushrooms include lectins, terpenes, terpenoids, polysaccharides, and fungal immunomodulatory proteins (FIPs). The distribution of these compounds varies from one species of mushroom to another, and their immunomodulatory activities depend on the core structures and chemical modifications in the composition of the fractions. In this review, we describe active compounds from medical mushrooms. We summarize potential mechanisms for their in vitro and in vivo activities and detail approaches used in developing and applying bioactive compounds from mushrooms. Finally, we discuss applications of fungal peptides and highlight areas that require improvement before the widespread use of those compounds as therapeutic agents and explore the status of clinical studies on the immunomodulatory activities of mushrooms and their products, as well as the prospect of clinical application of AMPs as 'drug-like' compounds with great potential for treatment of non-healing chronic wounds and multiresistant infections. [ABSTRACT FROM AUTHOR]

In order to improve the stability and functional properties of casein-derived bioactive peptides (CP) in yogurt, the peptides were microencapsulated using sodium alginate and sucrose fatty acid esters as the wall material, which was determined based on encapsulation efficiency and peptide loading, and the developed microcapsules were applied in yogurt. Scanning electronic microscopy (SEM), Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD) and differential scanning calorimetry (DSC) proved the successful encapsulation of the peptides. The microcapsules had good sustained release properties, and the release rate was (62.57 ± 1.17)% after 3 h of intestinal digestion. The microencapsulated bioactive peptides improved the water-holding capacity, hardness and viscosity of yogurt, and the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging ability of yogurt with the bioactive peptides was (63.73 ± 1.97)%. The microencapsulated bioactive peptides were not degraded during yogurt fermentation by lactic acid bacteria, and the functional properties of yogurt were enhanced by addition of the bioactive peptides.

Abstract Cardiovascular diseases (CVDs) affect the quality of life or are fatal in the worst cases, resulting in a significant economic and social burden. Therefore, there is an urgent need to invent functional products or drugs for improving patient health and alleviating and controlling these diseases. Marine bioactive peptides reduce and control CVDs. Many of the predisposing factors triggering CVDs can be alleviated by consuming functional foods containing marine biopeptides. Therefore, improving CVD incidence through the use of effective biopeptide foods from marine sources has attracted increasing interest and attention. This review reports information on bioactive peptides derived from various marine organisms, focusing on the process of the separation, purification, and identification of biological peptides, biological characteristics, and functional food for promoting cardiovascular health. Increasing evidence shows that the bioactivity and safety of marine peptides significantly impact their storage, purification, and processing. It is feasible to develop further strategies involving functional foods to treat CVDs through effective safety testing methods. Future work should focus on producing high‐quality marine peptides and applying them in the food and drug industry.

The production of bioactive peptides (BPs) usually involves the enzymatic hydrolysis stage during which one or more proteases are used to break down the parental protein into shorter fragments. In this review, efforts were made to focus on using pepsin as a unique protease capable of generating BPs. We started with the description of BPs and proteases prior to the unraveling of pepsin's properties and immobilization for the production of BPs. The peptic hydrolysis of food-derived proteins to generate BPs with biological functions, e.g. antioxidative, ACE-inhibitory, metal-binding, antidiabetic, anti-inflammatory, and antimicrobial activities from vegetable, fish, seafood, whey, casein, blood plasma, and egg proteins, among other unconventional protein sources were discussed. The review concluded with BPs used in developing food products for their techno-functional properties such as emulsifying, water, and fat-holding capacities. [ABSTRACT FROM AUTHOR]

Abstract In recent decades, the food system has been faced with the significant problem of increasing food waste. Therefore, the feed industry, supported by scientific research, is attempting to valorise the use of discarded biomass as co-products for the livestock sector, in line with EU objectives. In parallel, the search for functional products that can ensure animal health and performances is a common fundamental goal for both animal husbandry and feeding. In this context, camelina cake (CAMC), cardoon cake (CC) and cardoon meal (CM), due valuable nutritional profile, represent prospective alternatives. Therefore, the aim of this work was to investigate the antioxidant activity of CAMC, CC and CM following in vitro digestion using 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), Ferric reducing antioxidant power (FRAP) and oxygen radical absorbance capacity (ORAC) assays. Total phenolic content (TPC) and angiotensin converting enzyme (ACE) inhibitory activity, actively involved in modulating antioxidant properties, were also studied. Further, a peptidomic analysis was adopted to substantiate the presence of bioactive peptides after in vitro digestion. The results obtained confirmed an interesting nutritional profile of CAMC, CC and CM and relevant antioxidant and ACE inhibitory activities. In particular, considering antioxidant profile, CM and CC revealed a significantly higher (10969.80 ± 18.93 mg TE/100 g and 10451.40 ± 149.17 mg TE/100 g, respectively; p

Abstract Food‐derived peptides have garnered significant attention in research due to their multifaceted functionalities, abundant availability, efficient utilization of agricultural by‐products, and environmentally sustainable preparation methods. These peptides play a crucial role in human health, yet their precise mechanisms of action remain largely unexplored, posing challenges in their screening, preparation, and effective application utilizing protein‐based raw materials. This review offers an extensive examination of 19 types of bioactive peptides derived from food. The sources of food‐derived bioactive peptides are well concluded and the classifications are made according to their potential health benefit based on five primary systems: general bodily functions, the nervous system, the cardiovascular system, the metabolic system, and the immune system. This review specifically highlights the multifaceted impacts of tasty peptides on human health, extending beyond their gustatory effects. Furthermore, it explores the interplay between various functions of bioactive peptides, noting a progression from basic to advanced functionalities. Antioxidant activity and the modulation of key enzymes are identified as fundamental actions that are interconnected with other functional properties. This implies that a single bioactive peptide could exhibit multiple beneficial effects. The key role of antioxidant capabilities is underscored based on their broad influence and straightforward assessment. This comprehensive analysis aims to deepen the systematic understanding of the diverse benefits offered by various food‐derived peptides.

Objective Although pork loins is not a tough meat, they need to develop meat products with a soft texture for the elderly. This study focused on the physicochemical properties and tenderness characteristics of pork loin injected with green kiwifruit juice (GRJ) and gold kiwifruit juice (GOJ) during various incubation times. In addition, the antioxidant activities of hydrolysate derived from the hydrolysis of pork loin by kiwifruit juice protease were evaluated. Methods The pork loin was injected with 10% and 20% GRJ and GOJ, under various incubation times (0, 4, 8, and 24 h). Then, the physicochemical properties and tenderness of pork loins were measured. 2,2- diphenyl-1-picrylhydrazyl radical scavenging activity and reducing power were conducted to determine hydrolysate’s antioxidant activities derived from pork loin’s hydrolysis by kiwifruit juice protease. Results GRJ had greater tenderizing ability than GOJ, even at the 10% addition. When kiwifruit juice was injected into pork loin, the tenderness increased with increasing incubation time. This was confirmed by the decrease in intensity of the myosin heavy chain (MHC) band in sodium dodecyl sulfate–polyacrylamide gel electrophoresis. In particular, the MHC band decreased at 8 h for both 10% GRJ and 20% GOJ and at 4 h for 20% GRJ alone. The highest myofibril fragmentation index and peptide solubility were observed in pork loin treated with 20% GRJ compared to the other treatments during incubation. The 10% GRJ and 20% GOJ treatments showed similar levels of antioxidant activity of the protein hydrolysates in pork loin, and 20% GRJ showed the highest activity among the treatments. Conclusion Kiwifruit juice had protease activity, and GRJ was more useful for tenderizing meat products than GOJ. Thus, GRJ at 10% could be a potential agent to tenderize and enrich the natural antioxidant activity through the proteolysis of pork loin.

In recent decades, the food system has been faced with the significant problem of increasing food waste. Therefore, the feed industry, supported by scientific research, is attempting to valorise the use of discarded biomass as co-products for the livestock sector, in line with EU objectives. In parallel, the search for functional products that can ensure animal health and performances is a common fundamental goal for both animal husbandry and feeding. In this context, camelina cake (CAMC), cardoon cake (CC) and cardoon meal (CM), due valuable nutritional profile, represent prospective alternatives. Therefore, the aim of this work was to investigate the antioxidant activity of CAMC, CC and CM following in vitro digestion using 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), Ferric reducing antioxidant power (FRAP) and oxygen radical absorbance capacity (ORAC) assays. Total phenolic content (TPC) and angiotensin converting enzyme (ACE) inhibitory activity, actively involved in modulating antioxidant properties, were also studied. Further, a peptidomic analysis was adopted to substantiate the presence of bioactive peptides after in vitro digestion. The results obtained confirmed an interesting nutritional profile of CAMC, CC and CM and relevant antioxidant and ACE inhibitory activities. In particular, considering antioxidant profile, CM and CC revealed a significantly higher (10969.80 ± 18.93 mg TE/100 g and 10451.40 ± 149.17 mg TE/100 g, respectively; p < 0.05) ABTS value than CAMC (9511.18 ± 315.29 mg TE/100 g); a trend also confirmed with the FRAP assay (306.74 ± 5.68 mg FeSO4/100 g; 272.84 ± 11.02 mg FeSO4/100 g; 103.84 ± 3.27 mg FeSO4/100 g, for CC, CM and CAMC, respectively). Similar results were obtained for TPC, demonstrating the involvement of phenols in modulating antioxidant activity. Finally, CAMC was found to have a higher ACE inhibitory activity (40.34 ± 10.11%) than the other matrices. Furthermore, potentially bioactive peptides associated with ACE inhibitory, anti-hypertensive, anti-cancer, antimicrobial, antiviral, antithrombotic, DPP-IV inhibitory and PEP-inhibitory activities were identified in CAMC. This profile was broader than that of CC and CM. The presence of such peptides corroborates the antioxidant and ACE profile of the sample. Although the data obtained report the important antioxidant profile of CAMC, CC, and CM and support their possible use, future investigations, particularly in vivo trials will be critical to evaluate and further investigate their effects on the health and performance of farm animals. [ABSTRACT FROM AUTHOR]

AbstractRecently, kafirins from white sorghum [Sorghum bicolor (L) Moench] grain have shown promise as a source of biopeptides with anti-skin aging effects (anti-inflammatory, antioxidant, and inhibition of photoaging-associated enzymes). This study employed response surface methodology (RSM) to optimize the extraction and enzymatic hydrolysis of kafirins (KAF) for the production of peptides with anti-skin aging properties. The optimization of conditions (reaction time and enzyme/substrate ratio) for liquefaction with α-amylase and hydrolysis of KAF with alcalase was performed using 32 complete factorial designs. Subsequently, ultrafiltered peptide extracts were obtained with molecular weights of 1–3 kDa (KAF-UF3) and lower than 1 kDa (KAF-UF1), which mainly contain hydrophobic amino acids (proline, leucine, isoleucine, phenylalanine, and valine) and peptide fractions with molecular weights of 0.69, 1.14, and 1.87 kDa. Consequently, the peptide extracts protected immortalized human keratinocytes (HaCaT cells) from ultraviolet B radiation (UVB)-induced damage by preventing the decrease and/or restoring the activity of antioxidant enzymes [superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px)]. Furthermore, KAF-UF3 and KAF-UF1 inhibited (20–29%) elastase and collagenase overactivity in UVB-exposed murine fibroblasts (3T3 cells). Thus, KAF-UF3 and KAF-UF1 exhibited behavior similar to that observed with glutathione (GSH), suggesting their potential as functional peptide ingredients in skincare products. [ABSTRACT FROM AUTHOR]

To fill the need for environmentally sensitive fluorescent unnatural amino acids able to operate in the red region of the spectrum, we have designed and synthesized Alared, a red solvatochromic and fluorogenic amino acid derived from the Nile Red chromophore. The new unnatural amino acid can be easily integrated into bioactive peptides using classical solid‐phase peptide synthesis. The fluorescence quantum yield and the emission maximum of Alared‐labeled peptides vary in a broad range depending on the peptide's environment, making Alared a powerful reporter of biomolecular interactions. Due to its red‐shifted absorption and emission spectra, Alared‐labeled peptides could be followed in living cells with minimal interference from cellular autofluorescence. Using ratiometric fluorescence microscopy, we were able to track the fate of the Alared‐labeled peptide agonists of the apelin G protein‐coupled receptor upon receptor activation and internalization. Due to its color‐shifting environmentally sensitive emission, Alared allowed for distinguishing the fractions of peptides that are specifically bound to the receptor or unspecifically bound to different cellular membranes. [ABSTRACT FROM AUTHOR]

Bioactive peptides derived from both exogenous and endogenous origins have been studied extensively to use their beneficial effects in humans and animals. Bioactive peptides exhibit beneficial bodily functions and contribute to a healthy gastrointestinal system by influencing barrier functions, immune responses, and gut microbiota. Gut microbiota is a diverse microbial community that significantly influences the overall well-being and homeostasis of the body. Factors such as diet, age, lifestyle, medication, and environmental circumstances can affect the composition and diversity of the gut microbiota. The disturbances or imbalances in the gut microbiota have been associated with various health problems. The interplays between bioactive peptides and gut microbiota are not fully understood, but bioactive peptides hold promise as modulators of the gut microbiota to promote gut health. Almost all the bioactive research on human health, including the development of therapeutics and nutritional interventions, uses cell culture, even though their direct biofunctional activities can only occur when absorbed in the intestine and into the blood system. This review focuses on the current understanding of bioactive peptides in gut microbiota and their impact and mechanisms on gut and human health. The novelty of this review lies in its comprehensive analysis of the multifaceted interactions between bioactive peptides and gut microbiota, integrating knowledge from diverse disciplines between microbiology and nutrition. By elucidating the underlying mechanisms and identifying current research gaps, this review offers an outlook on the potential of bioactive peptides in promoting gut health and shaping future therapeutic and nutritional interventions. [ABSTRACT FROM AUTHOR]

Marine products have gained popularity due to their valuable components, especially protein, despite generating significant waste. Protein hydrolysates are widely recognized as the most effective method for transforming these low-value raw materials into high-value products. Fish protein hydrolysate (FPH), sourced from various aquatic wastes such as bones, scales, skin, and others, is rich in protein for value-added products. However, the hydrophobic peptides have limitations like an unpleasant taste and high solubility. Microencapsulation techniques provide a scientific approach to address these limitations and safeguard bioactive peptides. This review examines current research on FPH production methods and their antioxidant and antibacterial activities. Enzymatic hydrolysis using commercial enzymes is identified as the optimal method, and the antioxidant and antibacterial properties of FPH are substantiated. Microencapsulation using nanoliposomes effectively extends the inhibitory activity and enhances antioxidant and antibacterial capacities. Nevertheless, more research is needed to mitigate the bitter taste associated with FPH and enhance sensory attributes. [ABSTRACT FROM AUTHOR]

Featured Application: This study investigates the possibility of using the probiotic strain Lactobacillus plantarum 299v to ferment legume-derived beverages to enhance their bioactive properties. It has practical relevance in the development of innovative functional foods, nutraceuticals, supplements, or pharmaceuticals. Moreover, this study may be significant for exploring novel plant-based foods and searching for alternative protein sources. The investigations suggest effective approaches to increase the use of pulses, promoting their consumption and significance in the food industry. There is a global need to explore alternative protein sources and develop new health-promoting plant-based products. This study aimed to produce beverages from organic seeds of chickpeas and green or red lentils and assess the potential of using L. plantarum 299v to ferment these beverages. Spectrophotometric methods were used to evaluate the ability of the beverages to neutralize 1,1-diphenyl-2-picrylhydrazyl radicals (DPPH•) and chelate Fe2+. Total dietary fiber (including soluble and insoluble fractions) and the protein profiles were compared among the tested legume-derived beverages. The observations were focused on reductions in pH levels, total extract content, dietary fiber, ash, and moisture levels in all the fermented legume products. Fermentation contributed to increased antioxidative activity in all the tested products. The strongest ability to chelate Fe2+ (58.33 ± 2.35%) was noted in non-fermented green lentil products, while green lentil beverages fermented for 72 h exhibited the highest value of free radical scavenging activity (88.44 ± 4.24 DPPH• inhibition %). Chickpea products fermented for 72 h displayed the highest count of viable bacterial cells at 7.0 ± 0.7 × 108 CFU/g, while those fermented for 48 h exhibited the greatest number (2764) of potential biopeptide sequences. These findings highlight the feasibility of using this probiotic strain to enhance the functional properties of legume-based beverages. [ABSTRACT FROM AUTHOR]

Obesity is acknowledged as a significant risk factor for cardiovascular disease, often accompanied by increased inflammation and diabetes. Bioactive peptides derived from marine animal proteins show promise as safe and effective anti-obesity agents by regulating adipocyte differentiation through the AMPK signaling pathway. Therefore, this study aims to investigate the anti-obesity and anti-diabetic effects of bioactive compounds derived from a Meretrix lusoria Protamex enzymatic hydrolysate (MLP) fraction (≤1 kDa) through a 6-week treatment (150 mg/kg or 300 mg/kg, administered once daily) in leptin receptor-deficient db/db mice. The MLP treatment significantly decreased the body weight, serum total cholesterol, triglycerides, and LDL-cholesterol levels while also exhibiting a beneficial effect on hepatic and serum marker parameters in db/db mice. A histological analysis revealed a reduction in hepatic steatosis and epididymal fat following MLP treatment. Furthermore, poor glucose tolerance was improved, and hepatic antioxidant enzyme activities were elevated in MLP-treated mice compared to db/db control mice. Western blot analysis showed an increased expression of the AMPK protein after MLP treatment. In addition, the expression of lipogenic genes decreased in db/db mice. These findings indicate that bioactive peptides, which are known to regulate blood glucose levels, lipid metabolism, and adipogenesis, could be beneficial functional food additives and pharmaceuticals. [ABSTRACT FROM AUTHOR]

AbstractBioactive peptides from vegetal sources have been shown to have functional properties as anti-inflammatory, antioxidant, antihypertensive or antidiabetic capacity. For this reason, they have been proposed as an interesting and promising alternative to improve human health. In recent years, the numerous advances in the bioinformatics field for in silico prediction have speeded up the discovery of bioactive peptides, also reducing the associated costs when using an integrated approach between the classical and bioinformatics discovery. This review aims to provide an overview of the evolution, limitations and latest advances in the field of bioinformatics and computational tools, and specifically make a critical and comprehensive insight into computational techniques used to study the mechanism of interaction that allows the explanation of plant bioactive peptide functionality. In particular, molecular docking is considered key to explain the different functionalities that have been previously identified. The assumptions to simplify such a high complex environment implies a degree of uncertainty that can only be guaranteed and validated by in vitro or in vivo studies, however, the combination of databases, software and bioinformatics applications with the classical approach has become a promising procedure for the study of bioactive peptides. [ABSTRACT FROM AUTHOR]

The investigation of collagen hydrolysates (CHs) is essential due to their widespread use in health, cosmetic, and therapeutic industries, attributing to the presence of bioactive dipeptides (DPs) and tripeptides (TPs). This study developed a novel targeted liquid chromatography–tandem mass spectrometry (LC-MS/MS) method with propyl chloroformate (PCF) derivatization to measure three bioactive peptides—Hydroxyprolyl-glycine (Hyp-Gly), Glycyl-prolyl-hydroxyproline (Gly-Pro-Hyp), and Prolyl-hydroxyproline (Pro-Hyp)—in CHs, with strong correlation coefficients (0.992, 1.000, and 0.995, respectively) and low limits of detection (LODs) of 1.40, 0.14, and 1.16 µM, respectively. Untargeted data-dependent acquisition (DDA) analyses measured peptide size distribution, while amino acid analysis assessed nutritional content. The analysis of ten commercial CHs revealed similar amino acid profiles but varied peptide lengths, indicating diverse hydrolysis conditions. Products with higher proportions of smaller peptides showed elevated levels of the targeted bioactive peptides, suggesting that a smaller peptide size may increase bioactivity. These findings can inform the optimization of CH supplements, providing consumers with detailed peptide content for more informed choices. Data are available via ProteomeXchange with the identifier PXD051699. [ABSTRACT FROM AUTHOR]