Proteins and Bioactive Peptides in Food: Extraction Techniques, Functional Characterization and Structural Characterization

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Physics and (Bio)Chemistry".

Deadline for manuscript submissions: 31 January 2027 | Viewed by 557

Editors

National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China
Interests: food-derived proteins; bioactive peptides; hydrogels

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Guest Editor
School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China
Interests: food processing and preservation; development and utilization of proteins
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Special Issue Information

Dear Colleagues,

Food proteins are important nutrients for human health and, thus, make significant contributions to the unique functions of different foods. Proteins and bioactive peptides derived from food sources are gaining considerable interest not only for their nutritional value but also for their functional applications in developing biodegradable materials, particularly edible films and coatings for food preservation. The research in this field revolves around three key stages: extraction, functional characterization and structural characterization. Advanced extraction techniques are employed to isolate native proteins or generate specific peptide sequences from various sources like whey protein, soy protein, algae protein, gelatin, zein, gluten and so on.

The ensuing functional analysis is essential for determining film-forming ability, solubility, emulsifying properties and gelation properties, as well as the especially vital antioxidant and antimicrobial activities. These bioactive properties are essential for creating "active" packaging that can extend the shelf life of food products. Structural characterization, e.g., analyzing secondary and tertiary structures via spectroscopy and microscopy, provides fundamental insights into the molecular interactions within the protein/peptide matrix. This understanding is key to connecting their inherent structure to the mechanical strength, barrier properties and controlled release of bioactive compounds in the resulting film.

Dr. Di Wu
Dr. Yinan Du
Guest Editors

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Keywords

  • food proteins
  • bioactive peptides
  • edible films
  • structural characterization
  • active packaging

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Published Papers (1 paper)

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Research

17 pages, 3619 KB  
Article
Identification and Characterization of Novel DPP-IV Inhibitory Peptides from Limnospira platensis Hydrolysates: Stability and Intestinal Permeability Evaluation
by Kota Ebato, Haruka Kobayashi, Hiroaki Tsutsumi, Yoko Iijima and Kenjiro Sugiyama
Foods 2026, 15(16), 2838; https://doi.org/10.3390/foods15162838 - 14 Aug 2026
Abstract
As the prevalence of type 2 diabetes increases rapidly, the demand for natural origin dipeptidyl peptidase-IV (DPP-IV) inhibitors with fewer side effects is increasing. In this study, protein-rich Limnospira platensis was investigated as a source of bioactive peptides to enhance its value as [...] Read more.
As the prevalence of type 2 diabetes increases rapidly, the demand for natural origin dipeptidyl peptidase-IV (DPP-IV) inhibitors with fewer side effects is increasing. In this study, protein-rich Limnospira platensis was investigated as a source of bioactive peptides to enhance its value as a functional food ingredient. Hydrolysates were prepared using three food-processing proteases, individually and in two-step combinations, followed by in silico analysis and peptide identification via liquid chromatography–tandem mass spectrometry. Subsequently, the thermal stability, gastrointestinal resistance, and intestinal permeability (using Caco-2 cells) of the identified peptides were evaluated. It was revealed that the Orientase 22BF digest exhibited high DPP-IV inhibitory activity. From the digest, three novel peptides—SPSPN (IC50 = 144.1 ± 2.2 μM), VPSV (IC50 = 93.6 ± 5.8 μM), and IPIGG (IC50 = 13.4 ± 2.3 μM)—were identified, exhibiting DPP-IV inhibitory potencies comparable to or higher than previously reported Limnospira-derived peptides. Although VPSV exhibited low epithelial permeability (Papp = 4.02 ± 0.69 × 10−8 cm/s), it remained stable under simulated gastrointestinal digestion conditions, suggesting potential local luminal inhibitory activity within the small intestine. Overall, these findings highlight Limnospira-derived VPSV as a promising functional ingredient candidate with high bioactivity and digestive stability. Full article
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