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Food-Derived Bioactive Peptides

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: 30 July 2025 | Viewed by 1571

Special Issue Editors


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Guest Editor
Instituto de Agroquímica y Tecnología de Alimentos (CSIC), Av. Catedratico Agustin Escardino, 7, 46980 Paterna, 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

E-Mail Website
Guest Editor
Instituto de Agroquímica y Tecnología de Alimentos (CSIC), Av. Catedratico Agustin Escardino, 7, 46980 Paterna, Valencia, Spain
Interests: meat; food chemistry; proteomics; by-products; bioactivity
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Food proteins constitute an excellent source of bioactive peptides that can improve human health. Bioactive peptides can be generated in a large variety of foods during their processing but can be also produced from food by-products through enzymatic hydrolysis or microbial fermentation. There is increasing scientific evidence regarding the health benefits of bioactive peptides. In fact, peptides have been found to exert biological activities such as antihypertensive, antioxidant, hypoglycaemic, anti-inflammatory, and anticholesterolemic effects, and have been used for the development of functional ingredients.

This Special Issue welcomes the submission of research papers, reviews and short communications related to bioactive peptides in foods or hydrolyzates in food by-products; the methods utilized for their extraction, concentration and purification; their structural and functional characterization; and the mechanisms of action that regulate their activity and reported health benefits. This Special Issue also welcomes the submission of studies regarding the bioavailability of particular bioactive peptides using simulated gastrointestinal digestion and intestinal transport, together with the confirmation of their health benefits. Finally, this Special Issue is interested in recent advances and challenges regarding the use of proteomics and peptidomics for the identification and quantitation of bioactive peptides.

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

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Keywords

  • peptides identification
  • peptides characterization
  • functional foods
  • biological activity
  • peptidomics
  • proteomics

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Published Papers (3 papers)

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Research

26 pages, 7095 KiB  
Article
Chemopreventive Effects of Bioactive Peptides Derived from Black Soldier Fly Larvae Protein Hydrolysates in a Rat Model of Early-Stage Colorectal Carcinogenesis
by Kwanchanok Praseatsook, Arpamas Vachiraarunwong, Kenji Sato, Sivamoke Dissook, Hideki Wanibuchi, Sirinya Taya, Rawiwan Wongpoomchai, Pornngarm Dejkriengkraikul, Min Gi and Supachai Yodkeeree
Int. J. Mol. Sci. 2025, 26(13), 5955; https://doi.org/10.3390/ijms26135955 - 20 Jun 2025
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Abstract
Bioactive peptides from black soldier fly larvae (BSFL) protein hydrolysates have gained attention for their health-promoting properties. Our previous study demonstrated the chemopreventive potential of BSFL hydrolysates prepared with Alcalase (ASBP-AH) in colon cancer cells; their in vivo efficacy has not been fully [...] Read more.
Bioactive peptides from black soldier fly larvae (BSFL) protein hydrolysates have gained attention for their health-promoting properties. Our previous study demonstrated the chemopreventive potential of BSFL hydrolysates prepared with Alcalase (ASBP-AH) in colon cancer cells; their in vivo efficacy has not been fully elucidated. This study evaluated the chemopreventive effects of ASBP-AH, processed by spray-drying (ASBP-AHS) or freeze-drying (ASBP-AHF), in a diethylnitrosamine (DEN) and 1,2-dimethylhydrazine (DMH)-induced rat model of early-stage colorectal carcinogenesis. Oral administration of ASBP-AHS or ASBP-AHF significantly reduced aberrant crypt foci (ACF) and downregulated PCNA, COX-2, and NF-κB expression, without affecting apoptosis. Furthermore, both treatments restored microbial species richness and shifted gut microbial diversity disrupted by carcinogen exposure. ASBP-AHS specifically enriched short-chain fatty acid (SCFA)-producing bacteria, while ASBP-AHF favored anti-inflammatory microbial signatures. Likewise, correlation analysis revealed positive associations between microbial changes and SCFA levels, particularly with ASBP-AHS. Peptidomic profiling identified identical peptides in both hydrolysates, including stable pyroglutamyl-containing sequences with potential anti-inflammatory and microbiota-modulating effects. These findings support the in vivo chemopreventive potential of ASBP-AH and its promise as a functional food ingredient for promoting gut health and reducing colorectal cancer risk. Full article
(This article belongs to the Special Issue Food-Derived Bioactive Peptides)
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14 pages, 3247 KiB  
Article
In Silico Screening and Identification of Functional Peptides from Yak Bone Collagen Hydrolysates: Antioxidant and Osteoblastic Activities
by Yali Wang, Yue Wang, Baishan Fang and Yousi Fu
Int. J. Mol. Sci. 2025, 26(10), 4570; https://doi.org/10.3390/ijms26104570 - 10 May 2025
Viewed by 423
Abstract
Collagen peptides are recognized for their diverse bioactivities; however, efficiently screening potent peptides from hydrolysates remains challenging. This study employed an integrated strategy that combined in silico antioxidant activity prediction and molecular docking to myeloperoxidase (MPO) to screen active peptides derived from yak [...] Read more.
Collagen peptides are recognized for their diverse bioactivities; however, efficiently screening potent peptides from hydrolysates remains challenging. This study employed an integrated strategy that combined in silico antioxidant activity prediction and molecular docking to myeloperoxidase (MPO) to screen active peptides derived from yak bone collagen hydrolysates. Focusing on low molecular weight peptides, containing motifs such as GVM, GLP, GPM, and GPQ, we identified nine antioxidant peptides (KC1–KC9). Their activities were validated through in vitro free radical scavenging assays, with peptide KC7 demonstrating superior performance. Furthermore, peptide KC7 promoted proliferation, differentiation, and mineralization in MC3T3-E1 cells by upregulating osteogenic markers such as Runx2 and osteocalcin, modulating the Wnt/β-catenin and PI3K/Akt pathways, and reducing the Bax/Bcl-2 ratio. These results highlight KC7’s dual capacity to mitigate oxidative stress and potentially reduce apoptotic susceptibility, thereby stimulating osteogenesis. This positions peptide KC7 as a promising candidate for bone regeneration and oxidative stress-related disorders. Moreover, this study underscores the effectiveness of integrating computational and experimental approaches for the discovery of multifunctional natural peptides. Full article
(This article belongs to the Special Issue Food-Derived Bioactive Peptides)
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20 pages, 1273 KiB  
Article
Optimization of Sequential Enzymatic Hydrolysis in Porcine Blood and the Influence on Peptide Profile and Bioactivity of Prepared Hydrolysates
by Cristina Moreno-Mariscal, Federico Moroni, Jaume Pérez-Sánchez, Leticia Mora and Fidel Toldrá
Int. J. Mol. Sci. 2025, 26(8), 3583; https://doi.org/10.3390/ijms26083583 - 10 Apr 2025
Viewed by 656
Abstract
The search for new alternatives for the revalorization of porcine blood is crucial due to the large quantities that are annually generated in slaughterhouses. In this study, a sequential enzymatic hydrolysis of pig blood was optimized using different combinations of the enzymes, namely, [...] Read more.
The search for new alternatives for the revalorization of porcine blood is crucial due to the large quantities that are annually generated in slaughterhouses. In this study, a sequential enzymatic hydrolysis of pig blood was optimized using different combinations of the enzymes, namely, Alcalase 4.0 L and Protana™ Prime, Flavourzyme 1000 L, and Protamex®, as a sustainable method for obtaining extracts rich in bioactive peptides. All the assayed hydrolysates exhibited different peptide profiles and showed in vitro antioxidant, hypoglycemic, and anti-inflammatory activity, although their values differed significantly depending on the type of hydrolysis in ABTS, FRAP, and ORAC assays, as well as in the determination of the inhibitory activity of DPP-IV, NEP, TACE, and MGL enzymes. The hydrolysate obtained by the combination of Alcalase 4.0 L, Flavourzyme 1000 L, and Protana™ Prime (AFPP) resulted in the highest hydrolysis degree (33.39 ± 0.98%), and its peptide profile reflected a higher amount of peptides < 3 kDa. This hydrolysate also obtained significantly higher values for ABTS and the inhibition of TACE and MGL. However, APP2 stood out in NEP inhibition (79.39 ± 3.91%), while APPP was notable for DPP-IV inhibition (43.02 ± 1.39%). The analysis of the hydrolysates using mass spectrometry in tandem allowed for the identification of those sequences that are potentially responsible for the biological activities determined, which were characterized using in silico bioinformatic tools. The results show the potential of using sequential enzymatic hydrolysis in porcine blood to obtain multifunctional peptides. Full article
(This article belongs to the Special Issue Food-Derived Bioactive Peptides)
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