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Impact of Thermal and Non-Thermal Technologies on Food Protein Structure...
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Impact of Thermal and Non-Thermal Technologies on Food Protein Structure and Functionality: Mechanisms and Applications

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

Deadline for manuscript submissions: 10 February 2026 | Viewed by 1757

Special Issue Editors

Dr. Ting Li

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Guest Editor
State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Jiangnan University, Wuxi, China
Interests: plant protein; physical modification; heat treatment; structural characterization; functional properties
Prof. Dr. Li Wang

E-Mail Website
Guest Editor
School of Food Science and Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China
Interests: nutritional composition; food protein modification; functional regulation mechanisms in rice; development of new functional food products; rice product innovation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Food proteins are essential, high-quality dietary components increasingly utilized in innovative food products due to their nutritional benefits. Derived from both animal and plant sources, food proteins often face challenges such as low water solubility and poor functional properties, limiting their application in food systems.

To overcome these drawbacks, novel processing technologies—both thermal and non-thermal—are being developed to enhance food protein functionality. A thorough understanding of how these technologies affect protein structure and functionality, including the underlying mechanisms and potential applications of modified proteins, is crucial for advancing their use in food products.

This Special Issue invites original research and reviews that focus on the mechanisms and potential applications of thermal and non-thermal technologies in modifying food protein structure and improving functionality.

Dr. Ting Li
Prof. Dr. Li Wang
Guest Editors

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
  • structural characterization
  • functionality
  • thermal technologies
  • non-thermal technologies

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Published Papers (2 papers)

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Research

17 pages, 752 KB  
Article
Effects of Selective Enzymatic Hydrolysis on Structural Properties and Gel Properties of Soybean Protein Isolate
by Zhijun Fan, Yue San, Saike Tang, Anhui Ren, Yuejiao Xing, Li Zheng and Zhongjiang Wang
Foods 2025, 14(22), 3892; https://doi.org/10.3390/foods14223892 - 14 Nov 2025
Viewed by 548
Abstract
Soybean protein isolate (SPI) gel has been demonstrated to exhibit suboptimal stability and a coarse texture. Selective enzymatic hydrolysis modification has been demonstrated to effectively enhance the functional properties and structural stability of the protein. The objective of this study was to modify [...] Read more.
Soybean protein isolate (SPI) gel has been demonstrated to exhibit suboptimal stability and a coarse texture. Selective enzymatic hydrolysis modification has been demonstrated to effectively enhance the functional properties and structural stability of the protein. The objective of this study was to modify SPI using alkaline protease and papain. The impact of selective enzymatic hydrolysis on SPI was examined through the analysis of hydrolysis degree (DH), particle size, and protein purity. A systematic exploration was conducted in order to investigate the structural and quality characteristics of SPI gel. Indicators such as secondary structure changes, texture characteristics, water-holding capacity (WHC), rheology, and microstructure were analyzed. The findings indicate that when the DH of the SPI solution is 1%, its particle size is reduced relative to that when DH is 0.5%. The SDS-PAGE results indicated that alkaline protease could hydrolyze most of the 7S and 11S components in SPI into shorter peptides, while papain retained more of the 7S and 11S components and generated peptides with larger molecular weights. Fourier-transform infrared (FT-IR) spectral analysis indicated that following the process of enzymatic modification, the contents of α-helix and β-sheet in the secondary structure of SPI increased, while the contents of β-turns and random coils decreased. In the context of gel performance, it has been demonstrated that papain-modified SPI, attributable to its elevated content of macromolecular peptides, manifests superior WHC, hardness, springiness, cohesiveness, chewiness, storage modulus (G), and microstructure in comparison to alkaline protease-modified gel. Concurrently, the gel performance of papain modified SPI is significantly superior to that of unmodified SPI gel. This research provides a significant theoretical foundation and practical reference for promoting the efficient application of SPI in the domain of food processing. Full article
(This article belongs to the Special Issue Impact of Thermal and Non-Thermal Technologies on Food Protein Structure and Functionality: Mechanisms and Applications)
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14 pages, 1844 KB  
Article
Formation and Structural Characteristics of Heating-Induced Amyloid Fibrils Derived from Rice Albumin at Different pH Values
by Ting Li and Li Wang
Foods 2025, 14(17), 3069; https://doi.org/10.3390/foods14173069 - 30 Aug 2025
Viewed by 1010
Abstract
The comparison of rice albumin (RA) after heat treatment at neutral and acidic conditions was investigated in this study. Compared to the decreased thioflavin T (ThT) intensity of RA at pH 2 during heating, the ThT intensity of RA at pH 7 increased [...] Read more.
The comparison of rice albumin (RA) after heat treatment at neutral and acidic conditions was investigated in this study. Compared to the decreased thioflavin T (ThT) intensity of RA at pH 2 during heating, the ThT intensity of RA at pH 7 increased throughout the process of fibrillization. After fibrillization, the ThT intensity of RA at pH 7 was significantly increased by 27%, 38% and 35% at the protein concentrations of 1%, 2% and 4%, respectively. In addition, worm-like fibrils with a contour length of 100–300 nm were formed after heating at neutral conditions, accompanied by an increased average particle size and structural re-arrangement. Furthermore, the fibril formation at pH 7 involved the enhancement of an ordered β-sheet structure. However, only spherical agglomerate with a larger average particle size (>2000 nm) was observed when RA was heated at pH 2, because excessive hydrolysis destroyed the fibril-core sequences of RA. Additionally, the low solubility and high hydrophobicity of RA at pH 2 were not conducive to the formation of fibrils. In a word, a neutral environment is suitable for RA-based fibril formation, which provides a new insight for its future uses in food products. Full article
(This article belongs to the Special Issue Impact of Thermal and Non-Thermal Technologies on Food Protein Structure and Functionality: Mechanisms and Applications)
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