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Food Protein and Peptides: Structural Characterization and Physicochemical Properties
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Food Protein and Peptides: Structural Characterization and Physicochemical Properties

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

Deadline for manuscript submissions: 18 May 2026 | Viewed by 822

Special Issue Editor

Prof. Dr. Guizhao Liang

E-Mail Website
Guest Editor
Bioengineering College, Chongqing University, Chongqing, China
Interests: development of functional foods; discovery of bioactive peptides; design of natural inhibitors; antioxidants; molecular interaction of functional factors
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The intricate relationship between the structure of food proteins and peptides and their functional properties is a cornerstone of food science, yet it remains an area demanding deeper exploration. With the growing demand for sustainable food sources, novel ingredients, and personalized nutrition, a precise understanding of protein and peptide structures is more critical than ever. This structural knowledge is the key to unlocking their potential in dictating techno-functional properties like gelation and emulsification, as well as their biological activities, including antioxidant, antimicrobial, and antihypertensive effects.

This Special Issue is launched to address this need. We aim to compile cutting-edge research that employs advanced analytical techniques—from spectroscopy and chromatography to bioinformatics, computational modeling and artificial intelligence—to elucidate the primary, secondary, tertiary, and quaternary structures of these molecules. By bringing together high-quality contributions, this Special Issue seeks to bridge the gap between structural insights and practical applications, fostering innovation in food processing, the development of functional foods, and the valorization of valuable protein sources for a healthier and more sustainable future.

Prof. Dr. Guizhao Liang
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

  • food protein
  • bioactive peptide
  • protein structure
  • structural characterization
  • functional properties
  • spectroscopy
  • bioinformatics
  • artificial intelligence
  • molecular interaction

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Further information on MDPI's Special Issue policies can be found here.

Published Papers (2 papers)

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Research

16 pages, 2583 KB  
Article
HemPepPred: Quantitative Prediction of Peptide Hemolytic Activity Based on Machine Learning and Protein Language Model–Derived Features
by Xiang Li, Wanting Zhao, Xiao Liang, Xinlan Zhuo, Shuang Yu and Guizhao Liang
Foods 2025, 14(23), 4143; https://doi.org/10.3390/foods14234143 - 3 Dec 2025
Viewed by 380
Abstract
Accurate prediction of hemolytic peptides is essential for peptide safety evaluation and therapeutic design; however, existing models remain constrained by limited accuracy and interpretability. To overcome these challenges, we propose a regression framework that integrates embeddings from a protein language model with handcrafted [...] Read more.
Accurate prediction of hemolytic peptides is essential for peptide safety evaluation and therapeutic design; however, existing models remain constrained by limited accuracy and interpretability. To overcome these challenges, we propose a regression framework that integrates embeddings from a protein language model with handcrafted amino acid descriptors. Specifically, sequence representations derived from the ESM2_t33 model are fused with physicochemical amino acid descriptor features, and key predictive variables are selected through a three-stage strategy involving variance filtering, F-test ranking, and mutual information analysis. The final ensemble model, composed of Random Forest, Extremely Randomized Trees, Gradient Boosting, eXtreme Gradient Boosting (XGBoost), and Ridge Regression, achieved a coefficient of determination (R2) of 0.57 and a correlation coefficient (R) of 0.76 on the test set, outperforming previous approaches. To enhance interpretability, we applied Shapley value analysis and the Calibrated_Explanation algorithm to quantify feature contributions and generate reliable sample-specific explanations. The trained model has been deployed online as HemPepPred, a tool for predicting hemolytic concentration (HC50) values, which provides a practical platform for rational peptide design and safety assessment. Full article
(This article belongs to the Special Issue Food Protein and Peptides: Structural Characterization and Physicochemical Properties)
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20 pages, 2356 KB  
Article
Effects of 2,2′-Azobis(2-amidinopropane) dihydrochloride (AAPH) on Functional Properties and Structure of Winged Bean Protein
by Wei Fang, Jianglin Li, Zhaoxia Qu, Jiabin Hu, Dongming Chen and Xingjian Huang
Foods 2025, 14(23), 4120; https://doi.org/10.3390/foods14234120 - 1 Dec 2025
Viewed by 358
Abstract
Background: The impact and regulation of protein oxidative modification on protein functional properties is a research hotspot in food processing. This study aimed to clarify the mechanism of free radical oxidation on the structure and function of winged bean protein. Methods: Winged bean [...] Read more.
Background: The impact and regulation of protein oxidative modification on protein functional properties is a research hotspot in food processing. This study aimed to clarify the mechanism of free radical oxidation on the structure and function of winged bean protein. Methods: Winged bean protein was treated with different concentrations of AAPH (0.04 mmol/L, 0.20 mmol/L, 1.00 mmol/L). The functional properties (solubility, surface hydrophobicity, zeta potential), oxidation degree indicators, and secondary and tertiary structures of winged bean protein were tested and characterized under different oxidation conditions. Results: Low-concentration (0.04 mmol/L) AAPH led to the decomposition of winged bean protein, with decreased particle size and increased surface hydrophobicity and solubility; medium-concentration (0.20 mmol/L) AAPH caused significant aggregation of winged bean protein, with decreased surface hydrophobicity and solubility; high-concentration (1.00 mmol/L) AAPH led to the rearrangement of winged bean protein aggregates, forming more soluble aggregates and increasing solubility. With the gradual increase in AAPH addition, the α-helix and random coil structures of winged bean protein showed a trend of first increasing and then decreasing, while the β-sheet structure showed a trend of first decreasing and then increasing, and the β-turn structure remained almost unchanged. Conclusions: Under mild oxidation conditions (AAPH = 0.04 mmol/L), the functional properties of winged bean protein could be optimized. However, under relatively strong oxidation conditions (AAPH > 0.20 mmol/L), the structural integrity and functionality of winged bean protein would be compromised. This study helps deepen our understanding of the oxidative modification mechanism of winged bean protein. Full article
(This article belongs to the Special Issue Food Protein and Peptides: Structural Characterization and Physicochemical Properties)
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