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

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: 31 July 2025 | Viewed by 2972

Special Issue Editor


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Guest Editor
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

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Keywords

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

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Published Papers (3 papers)

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Research

17 pages, 3270 KiB  
Article
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
Viewed by 379
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 [...] Read more.
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
24 pages, 5171 KiB  
Article
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
Viewed by 718
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 [...] Read more.
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
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14 pages, 1783 KiB  
Article
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
Viewed by 1272
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 [...] Read more.
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
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