Food Proteins: Extraction, Functions and Applications

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

Deadline for manuscript submissions: 31 January 2026 | Viewed by 1076

Special Issue Editors


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Guest Editor
College of Food Science and Engineering, Shandong Agricultural University, Tai’an 271018, China
Interests: plant protein; grain; nutrition; food storage; multi-omic analysis
College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, China
Interests: protein chemistry; bioactive ingredients; nanoparticales; nutrition; food component interactions; absorption
Special Issues, Collections and Topics in MDPI journals

E-Mail Website
Guest Editor
College of Food Science and Engineering, Shandong Agricultural University, Tai’an 271018, China
Interests: grain storage; food nutrition; food machinery; metabolomic analysis

Special Issue Information

Dear Colleagues,

Protein, one of the three nutrients essential for the human body, plays an important role in our daily diet. The extraction and processing of food-sourced protein is a task that cannot be ignored and that can be achieved by various methods. Food proteins can be extracted from different sources; however, the protein extraction process needs to be constantly evaluated to improve efficiency and achieve suitable levels of quality. Additionally, protein extraction and processing parameters can cause various changes in the physicochemical properties of proteins, which can further affect their functional properties, including emulsifying and foaming properties, water absorption capacity, oil absorption capacity, aroma fixation, etc. Proteins have many applications in the food industry, including isolated or hydrolyzed proteins, which play a crucial role in human and animal nutrition.

Given the above, this Special Issue focuses on the topic of “Food Proteins: Extraction, Functions and Applications”. The theme centres around, but is not limited to, the composition, structure and properties of animal- and plant-origin food proteins, protein extraction techniques, bioactive proteins and peptides and the functional properties of proteins (e.g., their surface properties, hydration properties, gel properties, etc.).

Dr. Yuqian Liu
Dr. Rui Yang
Dr. Jinguang Liu
Guest Editors

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Keywords

  • food proteins
  • extraction
  • bioactive proteins and peptides
  • functional properties
  • applications

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Published Papers (2 papers)

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Research

13 pages, 2880 KB  
Article
Temperature-Induced Structural Changes in Muscle Proteins from Giant Squid (Dosidicus gigas) Mantle: FT-IR, Circular Dichroism, and FE-SEM Analysis
by Miguel A. León-Heredia, Enrique Marquez-Rios, Francisco Cadena-Cadena, Hisila Santacruz-Ortega, Ignacio Alfredo Rivero-Espejel, Nathaly Montoya-Camacho and Iván J. Tolano-Villaverde
Foods 2025, 14(17), 2922; https://doi.org/10.3390/foods14172922 - 22 Aug 2025
Viewed by 333
Abstract
The giant squid (Dosidicus gigas) is an abundant marine species with high protein content, making it a promising resource for the food and biomaterial industries. This study aimed to investigate the effect of temperature (25–100 °C) on the structural changes in [...] Read more.
The giant squid (Dosidicus gigas) is an abundant marine species with high protein content, making it a promising resource for the food and biomaterial industries. This study aimed to investigate the effect of temperature (25–100 °C) on the structural changes in sarcoplasmic, myofibrillar, and stromal proteins isolated from squid mantle. Fourier-transform infrared spectroscopy (FT-IR) and circular dichroism (CD) were employed to monitor modifications in secondary structure, while field emission scanning electron microscopy (FE-SEM) was used to examine morphological characteristics. The FT-IR analysis revealed temperature-induced transitions in amide I, II, and A bands, indicating unfolding and aggregation processes, particularly in myofibrillar and stromal proteins. CD results confirmed a loss of α-helix content and an increase in β-sheet structures with rising temperature, especially above 60 °C, suggesting progressive denaturation. FE-SEM micrographs illustrated clear morphological differences: sarcoplasmic proteins displayed smooth, amorphous structures; myofibrillar proteins exhibited fibrous, porous networks; and stromal proteins presented dense and layered morphologies. These findings highlight the different thermal sensitivities and structural behaviors of squid muscle proteins and provide insight into their potential functional applications in thermally processed foods and bio-based materials. Full article
(This article belongs to the Special Issue Food Proteins: Extraction, Functions and Applications)
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19 pages, 3771 KB  
Article
Effect of Carboxymethyl Konjac Glucomannan on the Gel Properties of Silver Carp Surimi: A Study on the Regulatory Mechanism of Substitution Degree
by Wenli Yan, Zhihan Ouyang, Xiaoying Luo, Rankun Xiao, Siqiao Liao, Fatang Jiang, Yonghui Li, Shanbai Xiong, Tao Yin and Xiangwei Zhu
Foods 2025, 14(15), 2715; https://doi.org/10.3390/foods14152715 - 1 Aug 2025
Viewed by 349
Abstract
Freshwater surimi typically exhibits poor gel-forming capability and is prone to gel deterioration, limiting its applications in food products. This study successfully prepared silver carp surimi gels with improved gel strength and water-holding capacity (WHC) using carboxymethyl konjac glucomannan (CKGM) as a functional [...] Read more.
Freshwater surimi typically exhibits poor gel-forming capability and is prone to gel deterioration, limiting its applications in food products. This study successfully prepared silver carp surimi gels with improved gel strength and water-holding capacity (WHC) using carboxymethyl konjac glucomannan (CKGM) as a functional modifier. Furthermore, the regulatory mechanism of CKGM with different degrees of substitution (DS) on the gel properties of silver carp surimi was systematically investigated. Results demonstrated that DS significantly influenced gel strength, WHC, and microstructure. CKGM (DS = 0.21%) substantially enhanced the gel strength and WHC through strengthened hydrophobic interactions and hydrogen-bond networks. However, CKGM with a higher DS (0.41%) induced a steric hindrance effect, decreasing elastic modulus and WHC and resulting in a more porous gel network. Raman spectroscopy analysis revealed that CKGM facilitated the conformational transition of myofibrillar proteins from α-helix to β-sheet, thereby improving the density of the gel network. The study provides theoretical foundations and technical guidance for the quality improvement of surimi products. Full article
(This article belongs to the Special Issue Food Proteins: Extraction, Functions and Applications)
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