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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Bioactives and Nutraceuticals".

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 30704

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Dr. Leticia Mora

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CSIC, Instituto de Agroquímica y Tecnología de Alimentos, Avenida Agustin Escardino 7, 46980 Paterna, Valencia, Spain
Interests: meat; food chemistry; proteomics; by-products; bioactivity
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Fidel Toldrá

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Instituto de Agroquimica y Tecnologia de los Alimentos (CSIC), Valencia, Spain
Interests: food science and nutrition; bioactive peptides; food enzymes; nutrients in meat and fish; functional ingredients; bioactives from animal by-products; advanced analytical techniques
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Foods and food by-products constitute very good sources of bioactive peptides, which can be generated during processing but also through enzymatic hydrolysis or microbial fermentation. The scientific knowledge on bioactive peptides is progressing very fast and relevant benefits for human health such as antihypertensive, antioxidant, hypoglycaemic, antiinflammatory, and anticholesterolemic activities have been reported.
In this Special issue, we are encouraging the submission of research papers, reviews and short communications related to bioactive peptides in foods or food by-products hydrolyzates, and methods for their extraction and purification, their structural and functional characterization, and mechanisms of action that regulate their activity and support the reported health benefits. Studies about the bioavailability of particular bioactive peptides using simulated gastrointestinal digestion and intestinal transport together with the confirmation of their health benefits are also welcome. Finally, the most recent advances and challenges in the use of proteomics and peptidomics for the analysis of bioactive peptides will also be considered.

Dr. Leticia Mora
Prof. Dr. Fidel Toldrá
Guest Editors

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Keywords

bioactive peptides
food peptides
identification
characterization
quantification
functional foods
biological activity
bioavailability
peptidomics
proteomics

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Published Papers (11 papers)

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Editorial

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2 pages, 200 KiB

Open AccessEditorial

Special Issue: Food Bioactive Peptides

by Leticia Mora and Fidel Toldrá

Int. J. Mol. Sci. 2022, 23(24), 15985; https://doi.org/10.3390/ijms232415985 - 15 Dec 2022

Cited by 1 | Viewed by 1412

Abstract

This Special Issue of the International Journal of Molecular Sciences is focused on bioactive peptides in foods or hydrolyzates of food by-products, the methods for the extraction and purification of bioactive peptides, their structural and functional characterization, and the mechanisms of action that [...] Read more.

(This article belongs to the Special Issue Food Bioactive Peptides)

Research

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32 pages, 2992 KiB

Open AccessArticle

Health Beneficial Bioactivities of Faba Bean Gastrointestinal (In Vitro) Digestate in Comparison to Soybean and Pea

by Delphine Martineau-Côté, Allaoua Achouri, Janitha Wanasundara, Salwa Karboune and Lamia L’Hocine

Int. J. Mol. Sci. 2022, 23(16), 9210; https://doi.org/10.3390/ijms23169210 - 16 Aug 2022

Cited by 13 | Viewed by 3067

Abstract

Faba beans are a promising emerging plant-based protein source to be used as a quality alternative to peas and soy. In this study, the potential health beneficial activities of three Canadian faba bean varieties (Fabelle, Malik and Snowbird) were investigated after in vitro gastrointestinal digestion and compared to two commonly used legumes (peas and soy). The results revealed that the faba beans had a higher antioxidant activity than peas when assessed with the 2,2-diphenyl-1-picrylhydrazyl (DPPH) and the 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) assays, except for the Fabelle variety. In the oxygen radical absorbance capacity (ORAC) and the iron chelating assays, the faba beans had a lower antioxidant activity than soy. Interestingly, Fabelle and Snowbird showed a higher antioxidant effect than the peas and soy at the cellular level. The antihypertensive properties of Fabelle and Malik varieties were significantly higher than peas but lower than soy. The in vitro antidiabetic activity was higher for soy, but no differences were found at the cellular level. The faba bean peptides were further fractionated and sequenced by mass spectrometry. Eleven peptides with in silico predicted bioactivities were successfully identified in the faba bean digestate and support validating the health-promoting properties of peptides. The results demonstrate the bioactive potential of faba beans as a health-promoting food ingredient against non-communicable diseases. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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16 pages, 1948 KiB

Open AccessArticle

Multifunctional Analysis of Chia Seed (Salvia hispanica L.) Bioactive Peptides Using Peptidomics and Molecular Dynamics Simulations Approaches

by José E. Aguilar-Toalá, Abraham Vidal-Limon and Andrea M. Liceaga

Int. J. Mol. Sci. 2022, 23(13), 7288; https://doi.org/10.3390/ijms23137288 - 30 Jun 2022

Cited by 15 | Viewed by 3044

Abstract

Chia seed peptides (CSP) can be a source of multifunctional biopeptides to treat non-communicable diseases. However, interactions and binding affinity involved in targeting specific receptors remains unexplored. In this study, molecular simulation techniques were used as virtual screening of CSP to determine drug-like candidates using a multi-target-directed ligand approach. CSP fraction with the best bioactivities in vitro was sequenced. Then, a prediction model was built using physicochemical descriptors (hydrophobicity, hydrophilicity, intestinal stability, antiangiogenic, antihypertensive, and anti-inflammatory) to calculate potential scores and rank possible biopeptides. Furthermore, molecular dynamics simulations (MDS) and ensemble molecular docking analysis were carried out using four human protein targets (ACE, angiotensin converting enzyme; VEGF, vascular endothelial growth factor; GLUC, glucocorticoid and MINC, mineralocorticoid receptors). Five known-sequence peptides (NNVFYPF, FNIVFPG, SRPWPIDY, QLQRWFR, GSRFDWTR) and five de novo peptides (DFKF, DLRF, FKAF, FRSF, QFRF) had the lowest energy score and higher affinity for ACE and VEGF. The therapeutic effects of these selected peptides can be related to the inhibition of the enzymes involved in angiogenesis and hypertension, due to formation of stable complexes with VEGF and ACE binding sites, respectively. The application of MDS is a good resource for identifying bioactive peptides for future experimental validation. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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11 pages, 2035 KiB

Open AccessArticle

Nrf2-Activating Bioactive Peptides Exert Anti-Inflammatory Activity through Inhibition of the NF-κB Pathway

by Federica Tonolo, Alessandra Folda, Valeria Scalcon, Oriano Marin, Alberto Bindoli and Maria Pia Rigobello

Int. J. Mol. Sci. 2022, 23(8), 4382; https://doi.org/10.3390/ijms23084382 - 15 Apr 2022

Cited by 19 | Viewed by 2622

Abstract

Redox status and inflammation are related to the pathogenesis of the majority of diseases. Therefore, understanding the role of specific food-derived molecules in the regulation of their specific pathways is a relevant issue. Our previous studies indicated that K-8-K and S-10-S, milk and soy-derived bioactive peptides, respectively, exert antioxidant effects through activation of the Keap1/Nrf2 pathway. A crosstalk between Nrf2 and NF-κB, mediated by the action of heme oxygenase (HO-1), is well known. On this basis, we studied if these peptides, in addition to their antioxidant activity, could exert anti-inflammatory effects in human cells. First, we observed an increase of HO-1 expression in Caco-2 cells treated with K-8-K and S-10-S, following the activation of the Keap1/Nrf2 pathway. Moreover, when cells are treated with the two peptides and stimulated by TNF-α, the levels of NF-κB in the nucleus decreased in comparison with TNF-α alone. In the same conditions, we observed the downregulation of the gene expression of proinflammatory cytokines (IL1B, IL6, and TNF), while the anti-inflammatory cytokine gene, IL1RN, was upregulated in Caco-2 cells processed as reported above. Then, when the cells were pretreated with the two peptides and stimulated with LPS, a different proinflammatory factor, (TNF-α) was estimated to have a lower secretion in the supernatant of cells. In conclusion, these observations confirmed that Nrf2-activating bioactive peptides, K-8-K and S-10-S, exerted anti-inflammatory effects by inhibiting the NF-κB pathway. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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12 pages, 2077 KiB

Open AccessArticle

Investigating the Short Peptidome Profile of Italian Dry-Cured Ham at Different Processing Times by High-Resolution Mass Spectrometry and Chemometrics

by Andrea Cerrato, Sara Elsa Aita, Anna Laura Capriotti, Chiara Cavaliere, Angela Michela Immacolata Montone, Carmela Maria Montone and Aldo Laganà

Int. J. Mol. Sci. 2022, 23(6), 3193; https://doi.org/10.3390/ijms23063193 - 16 Mar 2022

Cited by 10 | Viewed by 2071

Abstract

Short peptides have been spiking interest owing to their significant contribution to the taste and functional properties of dry-cured ham. In this study, a suspect screening approach based on high-resolution mass spectrometry was employed for the comprehensive characterization of the short endogenous peptidome in dry-cured ham samples at different processing stages (14, 22, and 34 months). After careful manual spectra interpretation, a chemometric approach based on principal component analysis was employed for highlighting the differences between the three sets of samples. A total of 236 short peptide sequences was tentatively identified, including 173 natural short peptides and 63 sequences containing non-proteinogenic amino acids, the highest number ever reported for endogenous sequences in dry-cured ham. Samples in the latest processing stages presented a generally higher abundance of dipeptides, indicating residual proteolytic activity. Moreover, the several annotated modified short peptides, mainly pyroglutamination and lactoyl conjugation, allowed hypothesizing several reactions occurring over time. For the first time, several lactoyl-dipeptides were tentatively identified in dry-cured ham samples with maximum concentration in the late processing stage samples. The presented results significantly contribute to the understanding of the reaction involving short peptides that affect the sensory and functional properties of dry-cured ham. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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17 pages, 1849 KiB

Open AccessArticle

Identification and Quantitation of Bioactive and Taste-Related Dipeptides in Low-Salt Dry-Cured Ham

by Alejandro Heres, Marta Gallego, Leticia Mora and Fidel Toldrá

Int. J. Mol. Sci. 2022, 23(5), 2507; https://doi.org/10.3390/ijms23052507 - 24 Feb 2022

Cited by 17 | Viewed by 2576

Abstract

The reduction of salt in meat products influences the natural mechanisms of proteolysis occurring in their processing, and could affect the final characteristics of the product in terms of texture and flavor due to its effect on the activity of enzymes. In the present study, the quantitation of dipeptides PA, GA, VG, EE, ES, DA, and DG in low-salt Spanish dry-cured ham was carried out using a triple quadrupole mass spectrometry instrument. The developed methodology demonstrated the advantages of hydrophilic interaction liquid chromatography in the removal of salt as a clean-up/separation step before ionization. This resulted in a value of 44.88 μg/g dry-cured ham for GA dipeptide, and values ranging from 2 to 8 μg/g dry-cured ham for VG, EE, ES, DA, and DG dipeptides. PA showed the lowest concentration with a value of 0.18 μg/g dry-cured ham. These outcomes prove the remarkable activity of muscular dipeptidyl peptidases during dry-curing as well as confirming the presence of these dipeptides which are related to certain taste attributes (e.g., ‘bitter’ or ‘umami’). Such dipeptides have also been confirmed as anti-inflammatory and potential cardiovascular protectors using in vitro assays, with the advantage of dipeptides small size increases their chance to resist both gastrointestinal digestion and intestinal/bloodstream transport without being degraded or modified. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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9 pages, 507 KiB

Open AccessCommunication

Screening of Novel Bioactive Peptides from Goat Casein: In Silico to In Vitro Validation

by Ezequiel R. Coscueta, Patrícia Batista, José Erick Galindo Gomes, Roberto da Silva and Maria Manuela Pintado

Int. J. Mol. Sci. 2022, 23(5), 2439; https://doi.org/10.3390/ijms23052439 - 23 Feb 2022

Cited by 25 | Viewed by 3189

Abstract

Food-derived bioactive peptides are of great interest to science and industry due to evolving drivers of food product innovation, including health and wellness. This study aims to draw attention through a critical study on how bioinformatics analysis is employed in the identification of bioactive peptides in the laboratory. An in silico analysis (PeptideRanker, BIOPEP, AHTpin, and mAHTPred) of a list of peptides from goat casein hydrolysate was performed to predict which sequences could potentially be bioactive. To validate the predictions, the in vitro antihypertensive potential of the five peptides with the highest potential was first measured. Then, for three of these, gastrointestinal digestion was simulated in vitro, followed by the analysis of the resulting ACE inhibitory activity as well as antioxidant capacity. We thus observed that the use of new computational biology technologies to predict peptide sequences is an important research tool, but they should not be used alone and complementarity with various in vitro and in vivo assays is essential. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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13 pages, 3052 KiB

Open AccessArticle

Disaggregation of Islet Amyloid Polypeptide Fibrils as a Potential Anti-Fibrillation Mechanism of Tetrapeptide TNGQ

by Raliat O. Abioye, Ogadimma D. Okagu and Chibuike C. Udenigwe

Int. J. Mol. Sci. 2022, 23(4), 1972; https://doi.org/10.3390/ijms23041972 - 10 Feb 2022

Cited by 12 | Viewed by 3012

Abstract

Islet amyloid polypeptide (IAPP) fibrillation has been commonly associated with the exacerbation of type 2 diabetes prognosis. Consequently, inhibition of IAPP fibrillation to minimize β-cell cytotoxicity is an important approach towards β-cell preservation and type 2 diabetes management. In this study, we identified three tetrapeptides, TNGQ, MANT, and YMSV, that inhibited IAPP fibrillation. Using thioflavin T (ThT) fluorescence assay, circular dichroism (CD) spectroscopy, dynamic light scattering (DLS), and molecular docking, we evaluated the potential anti-fibrillation mechanism of the tetrapeptides. ThT fluorescence kinetics and microscopy as well as transmission electron microscopy showed that TNGQ was the most effective inhibitor based on the absence of normal IAPP fibrillar morphology. CD spectroscopy showed that TNGQ maintained the α-helical conformation of monomeric IAPP, while DLS confirmed the presence of varying fibrillation species. Molecular docking showed that TNGQ and MANT interact with monomeric IAPP mainly by hydrogen bonding and electrostatic interaction, with TNGQ binding at IAPP surface compared to YMSV, which had the highest docking score, but interact mainly through hydrophobic interaction in IAPP core. The highly polar TNGQ was the most active and appeared to inhibit IAPP fibrillation by disaggregation of preformed IAPP fibrils. These findings indicate the potential of TNGQ in the development of peptide-based anti-fibrillation and antidiabetic nutraceuticals. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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15 pages, 1364 KiB

Open AccessArticle

Extended Cheese Whey Fermentation Produces a Novel Casein-Derived Antibacterial Polypeptide That Also Inhibits Gelatinases MMP-2 and MMP-9

by Maria Isabel Santos, Ana Lima, Joana Mota, Patrícia Rebelo, Ricardo Boavida Ferreira, Laurentina Pedroso, Maria Adélia Ferreira and Isabel Sousa

Int. J. Mol. Sci. 2021, 22(20), 11130; https://doi.org/10.3390/ijms222011130 - 15 Oct 2021

Cited by 10 | Viewed by 2168

Abstract

Our previous works produced a whey fermentation methodology that yielded antibacterial activity and potential inhibition of matrix metalloproteases (MMP)-2 and -9. Here, we evaluated if these activities were due to fermentation-produced peptides. Prolonged fermentation was carried out in the presence of our specific lactic acid bacteria (LAB) consortium. LAB fermentation yielded a total of 11 polypeptides, which were predominantly produced after 6 days of fermentation. One which was derived from beat casein presented a particularly high antibacterial activity against food pathogenic bacteria and was more effective than standard food disinfectants. This polypeptide was further studied and was also found to be active against several strains of pathogenic bacteria, including methicillin-resistant Staphylococcus aureus (MRSA), in a dose-dependent manner. It also inhibited MMP-2 and MMP-9 whilst reducing HT29 cancer cell migration in vitro. Overall, this novel whey-derived polypeptide presents dual antibacterial and anti-inflammatory activity, revealing a strong potential to be used in functional foods or as a nutraceutical. Its identification and further characterization can open novel perspectives in the field of preventive/curative diets related to gut microbiota, gut inflammation, and cancer prevention, particularly if used in in vivo studies. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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17 pages, 1743 KiB

Open AccessArticle

Purification and Identification of Cholesterol Micelle Formation Inhibitory Peptides of Hydrolysate from High Hydrostatic Pressure-Assisted Protease Hydrolysis of Fermented Seabass Byproduct

by Guan-Wen Chen, Hong-Ting Victor Lin, Li-Wen Huang, Chia-Hua Lin and Yu-Hsin Lin

Int. J. Mol. Sci. 2021, 22(10), 5295; https://doi.org/10.3390/ijms22105295 - 18 May 2021

Cited by 14 | Viewed by 3001

Abstract

This research focuses on the proteolytic capacity of sea bass byproduct (SB) and their hypocholesterolemic activity via the cholesterol micelle formation (CMF) inhibition. SB was fermented with seven mixed lactic acid bacteria for 5 h at 42 °C. The lactic fermented SB was hydrolyzed with Protease N for 6 h under HHP to obtain the SB hydrolysates (HHP-assisted Protease N hydrolysis after fermentation, F-HHP-PN6). The supernatant was separated from the SB hydrolysate and freeze-dried. As the hydrolysis time extended to 6 h, soluble protein content increased from 187.1 to 565.8 mg/g, and peptide content increased from 112.8 to 421.9 mg/g, while inhibition of CMF increased from 75.0% to 88.4%. Decreasing the CMF inhibitory activity from 88.4% to 42.1% by simulated gastrointestinal digestion (FHHP-PN6 was further hydrolyzed by gastrointestinal enzymes, F-HHP-PN6-PP) reduced the CMF inhibitory activity of F-HHP-PN6. Using gel filtration chromatography, the F-HHP-PN6-PP was fractioned into six fractions. The molecular weight of the fifth fraction from F-HHP-PN6-PP was between 340 and 290 Da, and the highest inhibitory efficiency ratio (IER) on CMF was 238.9%/mg/mL. Further purification and identification of new peptides with CMF inhibitory activity presented the peptide sequences in Ser-Ala-Gln, Pro-Trp, and Val-Gly-Gly-Thr; the IERs were 361.7, 3230.0, and 302.9%/mg/mL, respectively. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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Review

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37 pages, 1482 KiB

Open AccessReview

Bioactive and Sensory Di- and Tripeptides Generated during Dry-Curing of Pork Meat

by Alejandro Heres, Leticia Mora and Fidel Toldrá

Int. J. Mol. Sci. 2023, 24(2), 1574; https://doi.org/10.3390/ijms24021574 - 13 Jan 2023

Cited by 7 | Viewed by 2768

Abstract

Dry-cured pork products, such as dry-cured ham, undergo an extensive proteolysis during manufacturing process which determines the organoleptic properties of the final product. As a result of endogenous pork muscle endo- and exopeptidases, many medium- and short-chain peptides are released from muscle proteins. Many of them have been isolated, identified, and characterized, and some peptides have been reported to exert relevant bioactivity with potential benefit for human health. However, little attention has been given to di- and tripeptides, which are far less known, although they have received increasing attention in recent years due to their high potential relevance in terms of bioactivity and role in taste development. This review gathers the current knowledge about di- and tripeptides, regarding their bioactivity and sensory properties and focusing on their generation during long-term processing such as dry-cured pork meats. Full article

(This article belongs to the Special Issue Food Bioactive Peptides)

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