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 705

Special Issue Editors

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

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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
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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

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Keywords

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

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Published Papers (1 paper)

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Research

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 579
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
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