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Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations

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A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Nutraceuticals, Functional Foods, and Novel Foods".

Deadline for manuscript submissions: closed (15 February 2026) | Viewed by 19248

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Dr. Luigia Pazzagli

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Department of Experimental and Clinical Biomedical Sciences, University of Florence, Firenze, Italy
Interests: proteins and peptides; amino acids; enzymology; protein purification techniques; protein characterization; anti-oxidant and anti-inflammatory molecules; plant defences
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Special Issue Information

Dear Colleagues,

We welcome the submission of work exploring bioactive hydrolysates and peptides derived from food proteins. Bioactive proteins and peptides that are derived from foods have recently shown tremendous potential for application as functional ingredients and nutraceuticals to enhance health and reduce the risk of disease. Following physiological gastrointestinal digestion or through the fermentation of foods, bioactive peptides can form and exert their beneficial force both at the intestinal level and, following absorption, at the level of different areas of the body. In recent years, the number of bioactive peptides has increased enormously, and data banks are freely accessible to recover the amino acid sequences and functions of peptides which have not, until now, been characterized. However, the purification of peptides obtained from hydrolyzed foods, as well as their production by fermentation, are often insufficient for producing a quantity of peptides useful for carrying out in vitro studies. Moreover, the daily quantity of food necessary to produce a systemic beneficial effect has been determined in very few cases. Therefore, production, characterization, and bioavailability studies on peptides from different sources are welcome in order to increase the knowledge on this leading topic. Manuscripts dealing with the setting up of foods, naturally enriched or added with peptides, are also welcome in the Special Issue.

Dr. Luigia Pazzagli
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 250 words) can be sent to the Editorial Office for assessment.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

bioactive peptides
antioxidant
anti-inflammatory
fermented foods
protein hydrolysates
bioavailability
structure/function relations
classification

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Published Papers (10 papers)

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Research

20 pages, 1648 KB

Open AccessArticle

A Novel Peptide Derived from Sea Buckthorn Leaves: Enzymatic Preparation, Dual Inhibitory Activity Against α-Glucosidase and DPP-IV, and Its Molecular Mechanism

by Xuwei Qin, Yuchong Peng, Yingqi Huang, Fang Wang and Jianfeng Guo

Foods 2026, 15(9), 1489; https://doi.org/10.3390/foods15091489 - 24 Apr 2026

Viewed by 280

Abstract

Sea buckthorn leaves are a relatively underutilised component of sea buckthorn processed products; however, various studies have indicated that they possess hypoglycaemic potential. Under alkaline solubilisation and acid-precipitation conditions, the extraction yield of sea buckthorn leaf protein (SLP) reached 19.33%. Trypsin was selected as the hydrolysing enzyme to extract SLPPs-T, with half-maximal inhibitory concentrations (IC₅₀) against α-glucosidase and DPP-IV of 0.1361 ± 0.017 mg/mL and 0.1286 ± 0.012 mg/mL, respectively. UV spectroscopy, Fourier transform infrared spectroscopy, circular dichroism spectroscopy and particle size analysis indicated that the secondary and microstructures of SLP underwent changes following its hydrolysis to SLPPs-T; following separation, purification, sequence identification and computer screening, two novel peptides, PM-8 and VG-11, were obtained; molecular docking, solid-phase synthesis and in vitro experiments confirmed that VG-11 exhibited superior inhibitory activity, with half-maximal inhibitory concentrations (IC₅₀) against α-glucosidase and DPP-IV of 0.3885 ± 0.015 mM and 0.2611 ± 0.021 mM, respectively. In summary, this study explored the potential of sea buckthorn leaf protein as a natural hypoglycaemic product through a combination of computational modelling and experimental methods, thereby significantly enhancing the value of sea buckthorn resources. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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17 pages, 1727 KB

Open AccessArticle

Discovery of Iron-Chelating Peptides from Lupinus mutabilis via Integrated Purification and In Silico Validation

by Zayra Vila-Santillán, David Campos, Ana Aguilar-Galvez, Sebastien Carpentier, Thomás Valente de Oliveira, Romina Pedreschi and Rosana Chirinos

Foods 2026, 15(8), 1318; https://doi.org/10.3390/foods15081318 - 10 Apr 2026

Viewed by 406

Abstract

This study evaluated the iron-chelating capacity (ICC) of Lupinus mutabilis protein hydrolysate (LMPH) and its peptide fractions obtained through ultrafiltration and purification by immobilized metal ion affinity chromatography (IMAC) and gel filtration chromatography (GFC). Peptides were identified by LC-MS/MS, and their interactions with Fe²⁺ were analysed using molecular docking. LMPH was produced by enzymatic hydrolysis with Alcalase and subsequently subjected to ultrafiltration to concentrate peptides smaller than 2 kDa. This fraction exhibited higher ICC (35.1 mg Fe²⁺·g⁻¹) than the hydrolysate (22.75 mg Fe²⁺·g⁻¹). Sequential purification by IMAC and GFC yielded peptide fractions with enhanced ICC values (45.20 and 13.51 mg Fe²⁺·g⁻¹). A total of 176 peptides were identified by de novo LC-MS/MS sequencing, from which nine were selected based on favourable structure–ICC relationships and absence of predicted toxicity. Molecular docking analysis suggested spatial proximity between Fe²⁺ and the selected peptides. Although stable multi-site binding was not predicted under the applied computational model, the results support the potential of these sequences to interact with Fe²⁺. These findings provide molecular and chemical insights supporting the iron-binding potential of LMPH-derived peptides and highlight their future potential as functional ingredients for preventing and managing iron deficiency. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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23 pages, 14514 KB

Open AccessArticle

Preparation, Separation, and Identification of Low-Bitter ACE-Inhibitory Peptides from Sesame (Sesamum indicum L.) Protein

by Xin Lu, Cong Jia, Lixia Zhang, Xiaojing Sun, Guohui Song, Qiang Sun and Jinian Huang

Foods 2026, 15(2), 279; https://doi.org/10.3390/foods15020279 - 12 Jan 2026

Cited by 1 | Viewed by 707

Abstract

To prepare and characterize low-bitter angiotensin-converting enzyme (ACE)-inhibitory peptides from sesame protein, a triple-enzyme hydrolysis system was optimized using mixture design and response surface methodology. The resulting hydrolysate was separated by ultrafiltration and medium-pressure chromatography, followed by identification through nano-liquid chromatography–electrospray ionization-tandem mass spectrometry. Finally, the mechanism of typical low-bitter ACE-inhibitory peptides was elucidated by molecular docking and molecular dynamics simulation. Results showed that the optimal enzyme activity ratio of 1:0.94:1.07 for Alcalase, trypsin, and Flavourzyme, combined with optimized hydrolysis conditions (E/S ratio of 126,793.03 nkat/g, pH 8.40, 4.82 h hydrolysis time, and 45 °C), resulted in a peptide yield of 93.19 ± 0.14%, ACE-inhibitory rate of 95.92 ± 0.23%, and bitter value of 3.15 ± 0.09. APQLGR and APWLR exhibited high ACE-inhibitory activity and minimal bitterness among the seventeen identified peptides. Although both peptides bound to the S1 pocket and Zn²⁺ catalytic site of ACE, APWLR exhibited an additional interaction with the S2 pocket. Both peptides were predicted to antagonize the bitter taste receptor T2R14 by forming stable complexes with key residues, but two complexes exhibited distinct mechanisms of stabilization. This work demonstrates a method for producing dual-functional peptides from sesame protein, paving the way for their application in functional foods. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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21 pages, 1869 KB

Open AccessArticle

Sourdough Breads Made with Selected Lactobacillus Strains and Spelt Flour Contain Peptides That Positively Impact Intestinal Barrier

by Costanza Cicchi, Manuela Leri, Monica Bucciantini, Viola Galli, Simona Guerrini, Ángela Jiménez-Ortas, Diego Ceacero-Heras, Olga Martínez-Augustín, Luigia Pazzagli and Simone Luti

Foods 2025, 14(18), 3184; https://doi.org/10.3390/foods14183184 - 12 Sep 2025

Cited by 1 | Viewed by 1588

Abstract

Cereal grains have been dietary staples for millennia, providing essential nutrients alongside their primary carbohydrate content. Recently, the search for sustainable, nutrient-rich alternatives has drawn attention to spelt (Triticum aestivum ssp. spelta L.), a low-input crop with promising nutritional properties. Spelt supplies a higher content of unsaturated fatty acids and minerals, such as iron, zinc, and magnesium and exhibits lower levels of phytic acid compared to common wheat. This study explores the nutraceutical potential of fermented bakery products made from spelt and wheat flours using sourdough fermentation, a process driven by lactic acid bacteria (LAB) and yeasts. Breads produced with baker’s yeast were included for comparison. Specifically, this manuscript focuses on the generation of bioactive peptides (BPs), which have demonstrated anti-oxidant, anti-inflammatory, and gut-protective effects by modulating oxidative stress and inflammatory signaling pathways. By comparing aqueous extracts from breads prepared with varying flours and fermentation methods, optimal conditions for producing functional baked goods could be defined. The findings may offer new avenues for developing bakery products that potentially increase intestinal health while promoting sustainable agriculture through the use of spelt. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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15 pages, 1554 KB

Open AccessArticle

AOPxSVM: A Support Vector Machine for Identifying Antioxidant Peptides Using a Block Substitution Matrix and Amino Acid Composition, Transformation, and Distribution Embeddings

by Rujun Li, Haotian Wang, Qiunan Yu, Jing Cai, Liangzhen Jiang, Ximei Luo, Quan Zou and Zhibin Lv

Foods 2025, 14(12), 2014; https://doi.org/10.3390/foods14122014 - 6 Jun 2025

Cited by 1 | Viewed by 1585

Abstract

Antioxidant peptides (AOPs) have the natural properties of food preservatives; they are capable of improving the oxidation stability of food while also providing additional benefits such as disease prevention. Traditional experimental methods for identifying antioxidant peptides are time consuming and costly, so effective machine learning models are increasingly being valued by researchers. In this study, we integrated amino acid composition, transformation, and distribution (CTD) and block substitution matrix 62 (BLOSUM62) to develop an SVM-based AOP prediction model called AOPxSVM. This strategy significantly improves the prediction accuracy of the model by comparing 15 feature combinations and feature selection strategies, with their effectiveness being visually verified using UMAP. AOPxSVM achieves high accuracy values of 0.9092 and 0.9330, as well as Matthew’s correlation coefficients (MCCs) of 0.8253 and 0.8670, on two independent test sets, both surpassing the state-of-the-art methods based on the same test sets, thus demonstrating AOPs’ excellent identification capability. We believe that AOPxSVM can serve as a powerful tool for identifying AOPs. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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15 pages, 1047 KB

Open AccessArticle

Bioactive Peptides from Sodium Caseinate Hydrolysate with High Oral Absorption Regulate Blood Glucose in Type 2 Diabetic Mice via Inhibition of DPP-IV and Stimulation of GLP-1

by Pei-Yu Wu, Cheng-Hong Hsieh, Ali Iqbal, Yu-Shun Lin, Ming-Wei Cheng, Ling-Hsuan Chang, Shang-Ming Huang and Kuo-Chiang Hsu

Foods 2025, 14(11), 1953; https://doi.org/10.3390/foods14111953 - 30 May 2025

Cited by 4 | Viewed by 2508

Abstract

Type 2 diabetes mellitus remains a critical global health challenge, driving the pursuit of novel therapeutic strategies. This study investigated the anti-diabetic efficacy of the peptide 1CBR, derived from sodium caseinate hydrolysate, administered orally at 25 mg/kg/day to db/db mice over a 4-week period. Glucose tolerance was evaluated via oral glucose tolerance tests (OGTT), while plasma dipeptidyl peptidase-IV (DPP-IV) activity, glucagon-like peptide-1 (GLP-1), and insulin concentrations were quantified using enzyme-linked immunosorbent assays (ELISA). Two bioactive peptides, GPFPLPD and APDSGNFR, were isolated and characterized, exhibiting half-maximal inhibitory concentrations (IC₅₀) of 99.12 µM and 73.07 µM for DPP-IV inhibition, respectively, and both significantly stimulated GLP-1 secretion in enteroendocrine cells in vitro. Pharmacokinetic analysis in Sprague–Dawley rats demonstrated oral bioavailability of 11.28% and 19.12% for these peptides, surpassing typical expectations for peptide-based agents. Collectively, these results provide compelling evidence that 1CBR-derived peptides exert glucose-lowering effects through the dual mechanisms of DPP-IV inhibition and GLP-1 stimulation, combined with favorable oral absorption profiles. These findings underscore the potential of 1CBR peptides as promising candidates for development into nutraceuticals or pharmaceutical agents for diabetes management. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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19 pages, 3614 KB

Open AccessArticle

Immunoenhancement Function of the Novel Hexapeptide (LVVLGH) from Thick-Shelled Mussel (Mytilus coruscus) on Immunodeficient Mice by Activating the NF-κB/MAPK Pathway

by Xu Yang, Yu Zeng, Fandi Que, Shiqing Fu, Li Xu, Fangmiao Yu and Bin Wang

Foods 2025, 14(11), 1865; https://doi.org/10.3390/foods14111865 - 24 May 2025

Cited by 3 | Viewed by 1194

Abstract

A novel hexapeptide LVVLGH (LH-6) from the thick-shelled mussel (Mytilus coruscus) demonstrated potent immune-enhancing effects in RAW264.7 cells in vitro, but its immunological activity in vivo is unclear. As a result, the present study was designed to investigate the in vivo effects of LH-6 on cyclophosphamide-induced immunodeficient mice. The results demonstrate that LH-6 promoted the growth and development of immunodeficient mice in a concentration-dependent manner, remarkably elevated the immune organ index, and relieved the pathological characteristics of the spleen and thymus. Additional experiments also revealed that LH-6 effectively promoted the multiplication of splenic lymphocytes and natural killer activity, enhanced the function of abdominal macrophages, and apparently recovered delayed-type hypersensitivity in immunodeficient mice. The secretion of IgA, IgG, IgM, TNF-α, IL-1β, IL-6, and serum hemolysin were remarkably improved by LH-6, suggesting that LH-6 can synergistically strengthen cellular and humoral immunity. In addition, LH-6 promoted the phosphorylation of IκBα and nuclear translocation of p65, which correspondingly increased the phosphorylation levels of p38, JNK, and ERK; activated the NF-κB and MAPK pathways; and exerted in vivo immunomodulatory activities. Docking results show that LH-6 has favorable binding energies to candidate proteins in the NF-κB and MAPK pathways. To summarize, this research further demonstrated that LH-6 possesses in vivo immunomodulatory activity, which provides a possibility for the subsequent development of immune-enhancing functional foods. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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17 pages, 4110 KB

Open AccessArticle

Antioxidant Peptides from Hizikia fusiformis: A Study of the Preparation, Identification, Molecular Docking, and Cytoprotective Function of H₂O₂-Damaged A549 Cells by Regulating the Keap1/Nrf2 Pathway

by Shang Lv, Bin Hu, Su-Zhen Ran, Min Zhang, Chang-Feng Chi and Bin Wang

Foods 2025, 14(3), 400; https://doi.org/10.3390/foods14030400 - 26 Jan 2025

Cited by 39 | Viewed by 2964

Abstract

Hijiki (Hizikia fusiformis) is a seaweed native to warm-temperate and subtropical regions that has a high edible value and economic value, with a production of about 2 × 10⁵ tons/year. Current research has clearly shown that the pharmacological activities of active ingredients from hijiki have covered a broad spectrum of areas, including antioxidant, hypoglycemic, antiviral, anticoagulant, anti-inflammatory, intestinal flora modulation, anti-aging, antineoplastic and antibacterial, and anti-Alzheimer’s disease areas. However, no studies have reported on the production of antioxidant peptides from hijiki proteins. The objectives of this study were to optimize the preparation process and explore the cytoprotective function and mechanisms of antioxidant peptides from hijiki protein. The results indicated that papain is more suitable for hydrolyzing hijiki protein than pepsin, trypsin, alkaline protease, and neutral protease. Under the optimized parameters of an enzyme dosage of 3%, a material–liquid ratio of 1:30, and an enzyme digestion time of 5 h, hijiki hydrolysate with a high radical scavenging activity was generated. Using ultrafiltration and serial chromatographic methods, ten antioxidant oligopeptides were purified from the papain-prepared hydrolysate and identified as DGPD, TIPEE, TYRPG, YTPAP, MPW, YPSKPT, YGALT, YTLLQ, FGYGP, and FGYPA with molecular weights of 402.35, 587.61, 592.64, 547.60, 532.53, 691.77, 523.57, 636.73, 539.58, and 553.60 Da, respectively. Among them, tripeptide MPW could regulate the Keap1/Nrf2 pathway to significantly ameliorate H₂O₂-induced oxidative damage of A549 cells by increasing cell viability and antioxidant enzyme (SOD, CAT, and GSH-Px) activity, decreasing ROS and MDA levels, and reducing the apoptosis rate. Molecular docking experiments show that HFP5 (MPW) exerts its inhibitory effect mainly through hydrogen bonds and hydrophobic interactions with the Kelch domain of the Keap1 protein, eventually facilitating the translocation of Nrf2 to the nucleus. Therefore, antioxidant peptides from hijiki can be applied to develop algae-derived health foods for treating diseases associated with oxidative stress. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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24 pages, 5171 KB

Open AccessArticle

Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace Peptide

by Ying Mu, Ruxianguli Maimaitiyiming, Jingyang Hong, Yu Wang, Yao Zhao, Ruoqing Liu, Liang Wang, Keping Chen and Aihemaitijiang Aihaiti

Foods 2025, 14(2), 145; https://doi.org/10.3390/foods14020145 - 7 Jan 2025

Cited by 6 | Viewed by 3732

Abstract

The substantial quantity of discarded tomato pomace (TP) results in the waste of valuable resources. This study utilizes these tomato by-products by mixing them with water in a specific proportion and fermenting the mixture in two stages: first with yeast, and then with lactic acid bacteria. The most suitable microbial strains for TP fermentation were identified by evaluating parameters such as peptide content, degree of hydrolysis, and gel electrophoresis analysis. Subsequently, tomato pomace peptides (TPPs) were separated into peptides of different molecular weights using ultrafiltration. The IC₅₀ values, ACE inhibitory activities, and in vitro stability of these peptides were compared, and their secondary structures and microstructures were characterized. The results indicated that the soluble protein concentration increased from 26.25 mg/g to 39.03 mg/g after 32 h of fermentation with strain RV171. After an additional 32 h of fermentation with Bifidobacterium thermophilum, the peptide content reached 49.18 ± 0.43%. SDS-PAGE gel electrophoresis showed that the TPP molecular weights were predominantly below 10 kDa. The IC₅₀ results demonstrated that fractions with smaller molecular weights exhibited greater ACE inhibitory activities. Structural analysis confirmed that the TP hydrolysate was indeed a peptide. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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14 pages, 1783 KB

Open AccessArticle

Biological Activities of Soy Protein Hydrolysate Conjugated with Mannose and Allulose

by Artorn Anuduang, Sakaewan Ounjaijean, Rewat Phongphisutthinant, Pornsiri Pitchakarn, Supakit Chaipoot, Sirinya Taya, Wason Parklak, Pairote Wiriyacharee and Kongsak Boonyapranai

Foods 2024, 13(19), 3041; https://doi.org/10.3390/foods13193041 - 25 Sep 2024

Cited by 3 | Viewed by 2760

Abstract

The non-enzymatic conjugation of peptides through the Maillard reaction has gained attention as an effective method to enhance biological functions. This study focuses on two conjugate mixtures: crude soy protein hydrolysate (SPH) conjugated with mannose (SPHM) and crude soy protein hydrolysate conjugated with allulose (SPHA). These two mixtures were products of the Maillard reaction, also known as non-enzymatic glycation. In vitro experiments were conducted to evaluate the antioxidant, anti-pancreatic lipase, inhibition of Bovine Serum Albumin (BSA) denaturation, and anti-angiotensin converting enzyme (ACE) activities of these conjugated mixtures. The results indicate that conjugated mixtures significantly enhance the antioxidant potential demonstrated via the DPPH and FRAP assays. SPHA exhibits superior DPPH scavenging activity (280.87 ± 16.39 µg Trolox/mL) and FRAP value (38.91 ± 0.02 mg Trolox/mL). Additionally, both conjugate mixtures, at a concentration of 10 mg/mL, enhance the BSA denaturation properties, with SPHM showing slightly higher effectiveness compared to SPHA (19.78 ± 2.26% and 5.95 ± 3.89%, respectively). SPHA also shows an improvement in pancreatic lipase inhibition (29.43 ± 1.94%) when compared to the SPHM (23.34 ± 3.75%). Furthermore, both the conjugated mixtures and rare sugars exhibit ACE inhibitory properties on their own, effectively reducing ACE activity. Notably, the ACE inhibitory effects of the individual compounds and their conjugate mixtures (SPHM and SPHA) are comparable to those of positive control (Enalapril). In conclusion, SPHM and SPHA demonstrate a variety of bioactive properties, suggesting their potential use in functional foods or as ingredients in supplementary products. Full article

(This article belongs to the Special Issue Bioactive Peptides from Food-Derived: Preparation, Development and Functional Utilizations)

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