Advances in the Development of Proteins from Grains and Legumes

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

Deadline for manuscript submissions: 31 August 2025 | Viewed by 465

Special Issue Editor


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Guest Editor
School of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: grain food; plant protein; processing technology; food colloids; flavor research
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Special Issue Information

Dear Colleagues,

The world's growing population and the quest for healthy eating habits have led to a gradual increase in the demand for plant-based proteins. Meanwhile, grains and legumes serve as significant sources of edible proteins. Processing technologies must be selected and optimized in order to produce protein-rich foods from grains and legumes with high nutritional value and good functionality.

Therefore, this Special Issue, entitled "Advances in the Development of Proteins from Grains and Legumes", will be released soon. The aim is to explore the mechanisms by which processing methods modulate the quality of grain and legume proteins, investigate their application in high-quality food products, and understand the trends in the development of these proteins. The Special Issue will also be concerned with changes in the structure and flavor of grain and legume proteins during food processing, as well as the impact on their functional properties.

This Special Issue will focus on multidisciplinary collaborations to improve the bioavailability of grain and legume proteins, providing new ideas for more nutritious, healthy, and sustainable food production

Dr. Fengying Xie
Guest Editor

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Keywords

  • grain proteins
  • legume proteins
  • protein modification
  • bioactive peptides
  • techno-functional properties
  • functional foods
  • structure
  • flavor
  • nutritional benefits
  • bioavailability

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Published Papers (2 papers)

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Research

16 pages, 1599 KiB  
Article
Effect of pH-shifting on the Physicochemical Properties of Pea Proteins and Its Effect on the Texture of Hybrid Gels Formed with Casein Micelles
by Raiane Rodrigues da Silva, Luis Henrique de Paula Souza, Lucas Silva de Sousa, Laura Destro Rodrigues, Gustavo Schäfer Nogueira, Luis Gustavo Lima Nascimento and Antônio Fernandes Carvalho
Foods 2025, 14(16), 2887; https://doi.org/10.3390/foods14162887 - 20 Aug 2025
Viewed by 130
Abstract
Hybrid systems combining animal and plant proteins are promising for developing sustainable, high-protein foods. However, structural incompatibility between proteins like casein and pea protein hinders the formation of stable systems such as gels. This study explores pH-shifting (alkalization at pH 12 followed by [...] Read more.
Hybrid systems combining animal and plant proteins are promising for developing sustainable, high-protein foods. However, structural incompatibility between proteins like casein and pea protein hinders the formation of stable systems such as gels. This study explores pH-shifting (alkalization at pH 12 followed by neutralization) as an innovative strategy to improve pea protein functionality and compatibility in hybrid gels. Modified pea protein showed increased solubility, reduced particle size, higher zeta potential, and decreased intrinsic fluorescence intensity, indicating conformational changes and exposure of buried tryptophan residues. These structural changes influenced gel behavior depending on the protein ratio (casein/pea—80:20, 50:50, 20:80). Gels with higher pea content showed increased hardness and water-holding capacity, while in casein-rich gels, hardness decreased, likely due to altered protein–protein interactions. This is the first study to systematically apply pH-shifting to enhance the compatibility between pea protein and casein in high-protein gels, integrating structural and functional analyses. The results demonstrate the potential of pH-shifting as a sustainable and effective approach for improving plant protein performance in hybrid formulations. Full article
(This article belongs to the Special Issue Advances in the Development of Proteins from Grains and Legumes)
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16 pages, 10427 KiB  
Article
Comparative Analysis of Structural Characterisation and Gel Properties of Blended/Co-Precipitated Soy-Pea Dual-Protein
by Lu Wang, Xinyu Zhang, Xinhui Wang, Aiting Hui, Fengying Xie and Xia Wu
Foods 2025, 14(16), 2867; https://doi.org/10.3390/foods14162867 - 19 Aug 2025
Viewed by 167
Abstract
This study proposed a pH-driven co-precipitation strategy to overcome the limitations of traditional physical blending in functional improvement of a dual-protein system. The results demonstrated that, in comparison with the soy-pea blended protein (SPBP), the soy-pea co-precipitated protein (SPCP) showed a decrease in [...] Read more.
This study proposed a pH-driven co-precipitation strategy to overcome the limitations of traditional physical blending in functional improvement of a dual-protein system. The results demonstrated that, in comparison with the soy-pea blended protein (SPBP), the soy-pea co-precipitated protein (SPCP) showed a decrease in α-helix and β-sheet content, accompanied by in an increase in random coil structure. SPCP exhibited decreased fluorescence intensity, smaller particle size (from 392.2 to 176.1 nm) with increased absolute zeta-potential values (from −13.7 to −19.7 mV), reduced surface hydrophobicity (from 21,987.3 to 9744.8), and increased content of disulfide bonds. Structural optimization of SPCP significantly bolstered intermolecular interactions between SPI and PPI. Molecular docking simulations also validated the presence of abundant hydrophobic interactions and hydrogen bonds within in the blend system. These modifications significantly enhanced the solubility of SPCP (especially SPCP8.0). The rheological analysis further revealed that the storage modulus (G′) and loss modulus (G″) of SPCP8.0 were both higher than those of SPBP, while its tan δ was lower than that of SPBP, indicating synergistic interactions between proteins. These interactions contributed to the formation of a more stable three-dimensional network structure, thereby conferring it with superior gel properties. These findings provide theoretical foundations for improving the functional properties of plant-based dual-protein and their applications in plant-based meat production. Full article
(This article belongs to the Special Issue Advances in the Development of Proteins from Grains and Legumes)
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