Research and Application of Bioactive Peptides in Food

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Nutrition".

Deadline for manuscript submissions: 30 September 2025 | Viewed by 15278

Special Issue Editors

College of Food Science and Engineering, Jilin University, Changchun 130062, China
Interests: bioactive peptides; functional properties; functional foods
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Guest Editor Assistant
Department of Food Science and Engineering Doctor of Engineering, Jilin University, Changchun, China
Interests: food engineering; food science; technology food & nutrition

Special Issue Information

Dear Colleagues,

Food-borne bioactive peptides are a class of active small molecules derived from food proteins from a wide range of sources, including animal source proteins (poultry eggs, dairy, meat), plant source proteins (soybean, corn, rice, quinoa), marine biogenic proteins (fish, shellfish), etc. Currently, bioactive peptides have been proven to have a variety of physiological activities such as antioxidant, anti-inflammatory, hypotensive, hypoglycemic, and bacteriostatic properties, and they can play a role in many application scenarios such as digestion and metabolism, neuromodulation, and repair of damage. This review focuses on the preparation, isolation, activity identification, and application of bioactive peptides. This includes, but is not limited to, the preparation of peptides based on novel enzymes, directional separation of peptides with special structure, and the confirmation of new functions. The research of preventive and therapeutic effects and mechanisms of peptides on diseases is also welcomed.

Dr. Ting Zhang
Guest Editor

Dr. Siwen Lyu
Guest Editor Assistant

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Keywords

  • bioactive peptides
  • physiological activities
  • functional food
  • novel enzymes
  • therapeutic mechanisms
  • targets combination
  • peptides’ structure

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Published Papers (6 papers)

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Research

22 pages, 4408 KiB  
Article
Antidiabetic and Immunomodulatory Properties of Peptide Fractions from Sacha Inchi Oil Press-Cake
by Erwin Torres-Sánchez, Cristina Martínez-Villaluenga, Samuel Paterson, Blanca Hernández-Ledesma and Luis-Felipe Gutiérrez
Foods 2025, 14(7), 1231; https://doi.org/10.3390/foods14071231 - 31 Mar 2025
Viewed by 681
Abstract
Sacha inchi (SI) oil press-cake (SIPC), a by-product of the sacha inchi oil extraction process, represents a novel protein source with potential bioactive applications in food. In this study, a sacha inchi protein concentrate (SPC) derived from SIPC was subjected to simulated gastrointestinal [...] Read more.
Sacha inchi (SI) oil press-cake (SIPC), a by-product of the sacha inchi oil extraction process, represents a novel protein source with potential bioactive applications in food. In this study, a sacha inchi protein concentrate (SPC) derived from SIPC was subjected to simulated gastrointestinal digestion (SGID) using the INFOGEST 2.0 protocol. The resulting digests were fractionated by ultrafiltration (<3, 3–10, and >10 kDa), and the bioactive properties of the peptide fractions were evaluated. In vitro α-amylase inhibition was assessed, along with immunomodulatory markers (NO, IL-6, and TNF-α), in an ex vivo RAW 264.7 cell model. Both gastric and intestinal digests exhibited significant α-amylase inhibition (20–45%), with the <3 kDa intestinal fraction showing the highest inhibition (45% at 20 mg/mL). Both gastric and intestinal <3 kDa fractions reduced NO production in RAW 264.7 macrophages subjected to a lipopolysaccharide challenge. HPLC-MS/MS analysis facilitated de novo sequencing of the peptide fractions, identifying 416 peptides resistant to SGID through the find-pep-seq script, which were further assessed in silico for toxicity, allergenicity, and bioavailability, revealing no significant risks and potential drug-likeness development. Molecular docking simulations of three peptides (RHWLPR, RATVSLPR, and QLSNLEQSLSDAEQR) with α-amylase and four peptides (PSPSLVWR, RHWLPR, YNLPMLR, and SDTLFFAR) with the TLR4/MD-2 complex suggesting potential roles in α-amylase inhibition and anti-inflammatory activity, respectively. The findings suggest that SI protein concentrates could be used in functional foods to prevent starch breakdown through α-amylase-inhibiting peptides released during digestion, reduce blood glucose, and mitigate inflammation and oxidative tissue damage. Full article
(This article belongs to the Special Issue Research and Application of Bioactive Peptides in Food)
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26 pages, 2305 KiB  
Article
Pilot-Scale Production of Sericin-Derived Oligopeptides (SDOs) from Yellow Silk Cocoons: Peptide Characterization and Specifications
by Papungkorn Sangsawad, Surangkhanang Chumee, Phanthipha Laosam, Sittiruk Roytrakul, Sasikan Katemala and Manote Sutheerawattananonda
Foods 2025, 14(3), 500; https://doi.org/10.3390/foods14030500 - 5 Feb 2025
Cited by 1 | Viewed by 921
Abstract
Our previous research demonstrated the health benefits of sericin-derived oligopeptides (SDOs) from yellow silk cocoons, particularly their hypoglycemic and antihypertensive properties. This study aims to produce SDOs at a pilot scale, preparing them for large commercial production as a novel food ingredient, and [...] Read more.
Our previous research demonstrated the health benefits of sericin-derived oligopeptides (SDOs) from yellow silk cocoons, particularly their hypoglycemic and antihypertensive properties. This study aims to produce SDOs at a pilot scale, preparing them for large commercial production as a novel food ingredient, and investigates the impact of scale-up on their characteristics and specifications. We compared the productivity of SDOs generated from 25 L and 300 L batches via the hydrolysis of sericin using 5% Neutrase (E/S) at 50 °C for 4 h. The 300 L production scale outperformed the 25 L scale, achieving a hydrolysis degree (DH) of 8.63%, a solid recovery rate of 94.35%, and enhanced inhibitory actions for dipeptidyl peptidase IV (DPP-IV) and angiotensin-converting enzyme (ACE). The characterization of peptides was carried out in ultrafiltered SDOs. Peptides < 3 kDa demonstrated optimal enzyme inhibition and were then fractionated by size exclusion chromatography into nine distinct fractions. Of the nine fractions, F1, F8, and F9 had significant enzyme inhibitory activity. LC-MS/MS analysis revealed 32 unique peptide sequences, with YPDLPYH exhibiting significant dual inhibitory effects on both DPP-IV (IC50 1.35 mM) and ACE (IC50 18.10 μM). The maximum residue limit (MRL) for trace metals, pesticide residues, and microbiological contamination in SDOs complies with food regulations. SDOs exhibited stability at 4, 25, and 45 °C for six months, based on their physical characteristics and biological activity. Considering their investigated characteristics, SDOs could be manufactured at a pilot capacity and used as a functional food component in commercial applications designed to improve metabolic health. Full article
(This article belongs to the Special Issue Research and Application of Bioactive Peptides in Food)
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16 pages, 1816 KiB  
Article
Antioxidant Peptides from Sacha Inchi Meal: An In Vitro, Ex Vivo, and In Silico Approach
by Erwin Torres-Sánchez, Iván Lorca-Alonso, Sandra González-de la Fuente, Blanca Hernández-Ledesma and Luis-Felipe Gutiérrez
Foods 2024, 13(23), 3924; https://doi.org/10.3390/foods13233924 - 5 Dec 2024
Cited by 2 | Viewed by 1764
Abstract
Plant-derived antioxidant peptides safeguard food against oxidation, helping to preserve its flavor and nutrients, and hold significant potential for use in functional food development. Sacha Inchi Oil Press-Cake (SIPC), a by-product of oil processing, was used to produce Sacha Inchi Protein Concentrate (SPC) [...] Read more.
Plant-derived antioxidant peptides safeguard food against oxidation, helping to preserve its flavor and nutrients, and hold significant potential for use in functional food development. Sacha Inchi Oil Press-Cake (SIPC), a by-product of oil processing, was used to produce Sacha Inchi Protein Concentrate (SPC) in vitro, hydrolyzed by a standardized static INFOGEST 2.0 protocol. This study aimed to integrate in vitro, ex vivo, and in silico methods to evaluate the release of antioxidant peptides from SPC during gastrointestinal digestion. In vitro and ex vivo methods were used to investigate the antioxidant potential of SPC digests. Bioinformatics tools (find-pep-seq, AnOxPP, AnOxPePred-1.0, PepCalc, MLCPP 2.0, Pasta 2.0, PlifePred, Rapid Peptide Generator, and SwissADME) were employed to characterize antioxidant peptides. The gastric and intestinal digests exhibited higher ABTS and ORAC values than those of SPC. Under basal conditions, gastric digest fractions GD1, GD2, and GD3 (<3, 3–10, and >10 kDa, respectively), separated by ultrafiltration, significantly reduced the ROS levels in the RAW264.7 macrophages while, under LPS stimulation, GD1 (16 µg/mL) and GD2 (500 and 1000 µg/mL) reversed the induced damage. From the de novo peptidome determined, 416 peptides were selected based on their resistance to digestion. Through in silico tools, 315 resistant peptides were identified as antioxidants. Despite low predicted bioavailability, the peptides SVMGPYYNSK, EWGGGGCGGGGGVSSLR, RHWLPR, LQDWYDK, and ALEETNYELEK showed potential for extracellular targets and drug delivery. In silico digestion yielded the sequences SVMGPY, EW, GGGGCGGGGGVSS, PQY, HGGGGGG, GGGG, HW, and SGGGY, which are promising free radical scavengers with increased bioavailability. However, these hypotheses require confirmation through chemical synthesis and further validation studies. Full article
(This article belongs to the Special Issue Research and Application of Bioactive Peptides in Food)
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13 pages, 2150 KiB  
Article
Goat Milk Protein-Derived ACE Inhibitory Peptide SLPQ Exerts Hypertension Alleviation Effects Partially by Regulating the Inflammatory Stress of Endothelial Cells
by Shenghao Xing, Xiaotong Zhang, Tong Mu, Jianxin Cao, Ke Zhao, Bing Han and Xinyan Peng
Foods 2024, 13(21), 3392; https://doi.org/10.3390/foods13213392 - 25 Oct 2024
Cited by 2 | Viewed by 8435
Abstract
Hypertension has always posed a severe threat to people’s health. Food-derived angiotensin-converting enzyme (ACE)-inhibitory peptides have the potential to both prevent and treat hypertension. In the current investigation, two ACE-inhibitory peptides (SLPQ and PYVRYL) from goat milk were studied for their endothelial effects [...] Read more.
Hypertension has always posed a severe threat to people’s health. Food-derived angiotensin-converting enzyme (ACE)-inhibitory peptides have the potential to both prevent and treat hypertension. In the current investigation, two ACE-inhibitory peptides (SLPQ and PYVRYL) from goat milk were studied for their endothelial effects using EA.hy926 cells. PYVRYL outperformed SLPQ, yet neither impacted cell survival below 200 μg/mL. Investigation of SLPQ’s impact on EA.hy926 cell expression revealed 114 differentially expressed genes, with 65 downregulated and 49 upregulated. The genes were enriched in cytokine interactions, coagulation cascades, Hippo signaling, and ECM–receptor interaction. Decreased c-x-c motif chemokine ligand 2 (CXCL2), integrin subunit beta 2 (ITGB2), and fbj murine osteosarcoma viral oncogene homologue (FOS) expression and increased secreted phosphoprotein 1 (SPP1) expression may protect endothelial cells from inflammation. Our findings suggest that beyond ACE inhibition, SLPQ aids blood pressure control by influencing endothelial function, paving the way for its use as an antihypertensive food ingredient. Full article
(This article belongs to the Special Issue Research and Application of Bioactive Peptides in Food)
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15 pages, 2368 KiB  
Article
Potential Application of Egg White Peptides for Antioxidant Properties: Perspectives from Batch Stability and Network Pharmacology
by Siwen Lyu, Ting Li, Qi Yang, Jingbo Liu, Ting Zhang and Ting Yu
Foods 2024, 13(19), 3148; https://doi.org/10.3390/foods13193148 - 2 Oct 2024
Viewed by 1393
Abstract
This study investigated the batch stability of egg white peptides (EWPs) during the enzymatic hydrolysis process, and confirmed the potential application of four crucial four peptides inoxidative damage repair. The results revealed that different batches of EWPs had good stability relating to antioxidant [...] Read more.
This study investigated the batch stability of egg white peptides (EWPs) during the enzymatic hydrolysis process, and confirmed the potential application of four crucial four peptides inoxidative damage repair. The results revealed that different batches of EWPs had good stability relating to antioxidant activity. With a similar sequence to confirmed antioxidant peptides, four EWPs (QMDDFE, WDDDPTD, DEPDPL, and FKDEDTQ) were identified withhigh repetition rates, and their potential to repair oxidative damage was investigated. Network pharmacology results showed that these four peptides could regulate the targets related to oxidative damage. Enrichment results demonstrated that these four peptides could influence the targets and pathways related to glutathione transferase activity (enrichment score: 148.0) and glutathione metabolism (p value: 9.22 × 10−10). This study could provide evidence for the batch stability of hydrolyzed prepared EWPs, and offer theoretical support for the development of antioxidant damage ingredients derived from foods. Full article
(This article belongs to the Special Issue Research and Application of Bioactive Peptides in Food)
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21 pages, 30676 KiB  
Article
Combined Peptidomics and Metabolomics Analyses to Characterize the Digestion Properties and Activity of Stropharia rugosoannulata Protein–Peptide-Based Materials
by Wen Li, Wanchao Chen, Zhong Zhang, Di Wu, Peng Liu, Zhengpeng Li and Yan Yang
Foods 2024, 13(16), 2546; https://doi.org/10.3390/foods13162546 - 15 Aug 2024
Cited by 1 | Viewed by 1212
Abstract
Protein–peptide-based materials typically possess high nutritional value and various physiological regulatory activities. This study evaluated the digestion, metabolism, and activity of Stropharia rugosoannulata protein–peptide-based materials. After the S. rugosoannulata protein–peptide-based materials were digested (simulated) orally, in the stomach, and in the intestines, the [...] Read more.
Protein–peptide-based materials typically possess high nutritional value and various physiological regulatory activities. This study evaluated the digestion, metabolism, and activity of Stropharia rugosoannulata protein–peptide-based materials. After the S. rugosoannulata protein–peptide-based materials were digested (simulated) orally, in the stomach, and in the intestines, the proportions of >10,000 Da, 5000~10,000 Da, and <180 Da in the digestion products increased, and the peptide content was maintained at more than 120 mg/g dry weight. The digestion products of eight test groups with different oral–gastrointestinal digestion-level settings all had suitable ACE inhibitory activity (IC50 range 0.004~0.096 mg/mL). The main metabolite groups were lipid-like molecules, fatty acids, carboxylic acids, their derivatives, amino acids, peptides, and analogs. Bile and glycosylated amino acids were the main compounds that caused differences between groups. KEGG pathways enriched in differentially expressed metabolites included eight significantly upregulated pathways, including valine, leucine, and isoleucine biosynthesis, etc., and six significantly downregulated pathways, including the citric acid cycle (tricarboxylic acid cycle), etc. The arginine and proline metabolism pathways and the aminoacyl-tRNA biosynthesis pathways were upregulation and downregulation pathways that enriched multiple differentially expressed metabolites. Twenty-six metabolites, including bile acids, total bile acids, and the essential amino acids L-isoleucine and L-leucine, were differentially expressed metabolite markers of the protein–peptide-based material oral–gastrointestinal digestion products. Full article
(This article belongs to the Special Issue Research and Application of Bioactive Peptides in Food)
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