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Foods
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Effects of Processing on Protein Structure, Physicochemical Properties, and Function
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Effects of Processing on Protein Structure, Physicochemical Properties, and Function

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

Deadline for manuscript submissions: 30 September 2026 | Viewed by 3916

Special Issue Editors

Dr. Lifen Zhang

E-Mail Website
Guest Editor
College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China
Interests: protein processing; functional protein ingredients; innovative applications of proteins
Prof. Dr. Wenjun Wang

E-Mail Website
Guest Editor
College of Biosystems Engineering and Food Science, Zhejiang University, Hangzhou, China
Interests: novel approaches for food engineering; hydrocolloids; emulsions; protein processing; sonoprocessing; food packaging
Special Issues, Collections and Topics in MDPI journals
Dr. Dingyang Lv

E-Mail Website
Guest Editor Assistant
College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China
Interests: development and utilization of plant polysaccharide and protein resources

Special Issue Information

Dear Colleagues,

The need for protein is increasing due to the rapid growth of the global population, particularly those extracted from plant origin. Protein composition, extraction, purification, drying, and modification technologies affect aggregation, flexibility, molecular interactions, hydrophobic and charged surface groups, and functional properties of protein. For example, protein aggregation and unfolding occur to various extents depending on processing parameters (pH, temperature, and ionic strength) affecting final properties of protein-based foodstuffs. The protein structures affect its functional characteristics, including emulsifying, apparent viscosity, solubility, foaming, immunoreactivity, and gelling characteristics. These functional characteristics of proteins are factors of paramount importance in the food industry. It is expedient to develop a strategy to effectively utilize protein. Additionally, investigating how protein properties are affected by different composition and processing factors is crucial for food scientists to develop new products, optimize production processes, and ensure food nutrition and safety.

The aim of this Special Issue of Foods is to gather and display cutting-edge research on extraction, modification, and application technologies of proteins, including plants, animals, and microorganisms. This Special Issue welcomes original research articles and reviews on studying the processing technologies in tailoring protein structure, physicochemical properties, and function. Here, the processing technologies include ultrasound, pulsed electric field, hydrodynamic cavitation extraction, plasma treatment, tribo-electrostatic separation, extrusion, protein complexes with polysaccharides/polyphenols, and other novel technologies.

The scope of this Special Issue includes, but is not limited to, the following topics:  

  • Protein source, composition, and their relationship to its structure and functional propert.
  • Physical and other novel processing technology in tailoring protein.
  • Effects of processing on digestibility, allergenicity, and antinutritional factors of proteins.
  • Application of protein in meat, bakery products, dairy products, delivery systems, etc.

We look forward to receiving your contributions.

Dr. Lifen Zhang
Prof. Dr. Wenjun Wang
Guest Editors

Dr. Dingyang Lv
Guest Editor Assistant

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

  • protein
  • peptide
  • protein processing
  • protein structure
  • physicochemical properties
  • functional properties
  • conformation
  • aggregation and disaggregation
  • allergenicity

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

Published Papers (5 papers)

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Research

39 pages, 23169 KB  
Article
Study on the Effects of Polyphenols on the Properties, Microstructure, and Digestibility of Rice Protein Gel and the Interaction Mechanisms Between Polyphenols and Rice Protein
by Anna Wang, Mengran Fan and Ligen Wu
Foods 2026, 15(11), 1854; https://doi.org/10.3390/foods15111854 - 24 May 2026
Viewed by 183
Abstract
Rice protein has limited gelation properties, restricting its food applications. This study added four polyphenols—catechin (C), epicatechin (EC), tannic acid (TA), and proanthocyanidins (PC)—to rice protein to investigate their effects on gel rheology, in vitro digestibility, and microstructure. Multi-spectroscopy and molecular docking were [...] Read more.
Rice protein has limited gelation properties, restricting its food applications. This study added four polyphenols—catechin (C), epicatechin (EC), tannic acid (TA), and proanthocyanidins (PC)—to rice protein to investigate their effects on gel rheology, in vitro digestibility, and microstructure. Multi-spectroscopy and molecular docking were used to explore interaction mechanisms. During the temperature sweep (95 °C), PC- and TA-composite gels (GRP-PC, GRP-TA) showed storage moduli slightly higher than the pure rice protein gel (GRP), while GRP-C and GRP-EC (C- and EC-composite gels) were similar to GRP. In frequency sweep (25 °C), GRP had the highest modulus, followed by GRP-PC > GRP-TA > GRP-EC > GRP-C. Polyphenols reduced total digestibility (from 77.4% to 67.6–75.2%). All polyphenol-complexed gels showed markedly improved ABTS (2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)) and DPPH (2,2-diphenyl-1-picrylhydrazyl) radical scavenging activities. C and EC induced loosely crosslinked microstructures, whereas TA and PC formed sheet-like aggregates. Fluorescence quenching was predominantly static, with quenching rates TA > PC > EC > C. Binding constants followed the same order. Thermodynamic parameters (ΔH > 0, ΔS > 0, ΔG < 0) indicated hydrophobic interactions as the driving force. Molecular docking revealed that PC formed the most hydrogen bonds (8) with rice glutelin, followed by TA (4), C (5), and EC (3). These findings provide data support for designing rice protein-based functional foods. Full article
(This article belongs to the Special Issue Effects of Processing on Protein Structure, Physicochemical Properties, and Function)
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23 pages, 2306 KB  
Article
Ultrasonic and Glycation-Modified Soy Protein Isolate Delivery System Enhances the Antioxidant Activity of Antrodia cinnamomea Triterpenoids
by Qingya Ye, Hailun Xie, Jianing Dai, Qian Liu, Shiyao Jia and Huaxiang Li
Foods 2026, 15(5), 954; https://doi.org/10.3390/foods15050954 - 8 Mar 2026
Viewed by 526
Abstract
Antrodia cinnamomea is a rare medicinal and edible macrofungus, and its triterpenoids (ACT, A. cinnamomea triterpenoids) exhibit notable hepatoprotective, antioxidant, anticancer, and immunomodulatory activities. However, their poor aqueous solubility and low dispersibility in aqueous media have limited their practical applications. In this study, [...] Read more.
Antrodia cinnamomea is a rare medicinal and edible macrofungus, and its triterpenoids (ACT, A. cinnamomea triterpenoids) exhibit notable hepatoprotective, antioxidant, anticancer, and immunomodulatory activities. However, their poor aqueous solubility and low dispersibility in aqueous media have limited their practical applications. In this study, the conditions for ultrasonic treatment and xylo-oligosaccharide (XOS)-mediated glycation for soy protein isolate (SPI) were optimized; ACT was then encapsulated into the modified SPI carrier to prepare XOS-SPI-ACT nanoparticles. The delivery system was systematically characterized in terms of encapsulation efficiency (74.22 ± 2.15)%, drug-loading capacity (71.19 ± 4.67)%, storage stability, thermal stability, Fourier transform infrared (FTIR) spectroscopy, UV fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and surface morphological features. The results showed that ACT was effectively embedded in XOS-SPI to form a stable complex with excellent thermal stability and favorable storage stability over a 28-day period. The in vitro antioxidant activities of XOS-SPI-ACT, XOS-SPI, and free ACT were comparatively evaluated. XOS-SPI-ACT exhibited significantly higher scavenging capacities against DPPH radicals, ABTS radicals, hydroxyl radicals, and superoxide anions, as well as higher FRAP values (94%, 74%, 75%, 68%, and 2 mmol/g), compared with free ACT (48%, 17%, 21%, 32%, and 1 mmol/g). Furthermore, XOS-SPI-ACT effectively inhibited lipid peroxidation in the β-carotene/linoleic acid oxidation model, with an overall antioxidant performance of 72%, markedly higher than the 20% of free ACT. This study effectively improves the aqueous solubility and dispersibility of ACT, expands their application potential, and provides a foundation for developing ACT-based natural antioxidants and functional foods. Full article
(This article belongs to the Special Issue Effects of Processing on Protein Structure, Physicochemical Properties, and Function)
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24 pages, 3252 KB  
Article
Unveiling the Effects of Roasting Pre-Treatment on the Structural and Functional Properties of Lupinus angustifolius Protein Isolates and Their Impact on In Vitro Digestibility
by Niken Larasati Kusumawardani, Nurul Saadah Said and Won Young Lee
Foods 2026, 15(5), 914; https://doi.org/10.3390/foods15050914 - 6 Mar 2026
Viewed by 580
Abstract
This study investigates the effects of roasting pre-treatment on Lupinus angustifolius protein isolate (LPI) and the resulting structure–function relationships relevant to food applications. Lupin seeds were roasted for 0, 10, 20, and 30 min prior to protein extraction, and the resulting LPI was [...] Read more.
This study investigates the effects of roasting pre-treatment on Lupinus angustifolius protein isolate (LPI) and the resulting structure–function relationships relevant to food applications. Lupin seeds were roasted for 0, 10, 20, and 30 min prior to protein extraction, and the resulting LPI was characterized using circular dichroism (CD), Fourier-transform infrared (FT-IR) spectroscopy, intrinsic fluorescence spectroscopy, and SDS-PAGE. Unroasted LPI exhibited compact native conglutin structures with low solubility (58.64%), surface hydrophobicity (43.34 μg BPB), emulsifying activity (30.71 m2/g), and in vitro protein digestibility (IVPD, 82.84%). Roasting pre-treatment induced a biphasic structural response. Partial conformational changes increased solubility (up to 97.84%), exposed hydrophobic sites (peak 55.79 μg BPB), enhanced emulsifying activity (45.37 m2/g), doubled foaming capacity (210%), and improved IVPD (90.85%), likely due to structural changes that facilitated digestion. CD analysis showed a modest increase in α-helical content (3.43 → 6.74%) with minor fluctuations in β-sheet content, while fluorescence quenching indicated conformational loosening and partial reorganization. SDS-PAGE revealed the formation of soluble oligomers and high-molecular-weight aggregates, consistent with heat-induced association. Prolonged roasting reduced emulsion and foam stability because of aggregation, but maximized antioxidant capacity, likely associated with Maillard reaction products despite the observed depletion of amino acids. Overall, controlled roasting pre-treatment systematically modulates lupin protein structure and functionality, highlighting LPI as a competitive high-performance plant protein ingredient for food applications. Full article
(This article belongs to the Special Issue Effects of Processing on Protein Structure, Physicochemical Properties, and Function)
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19 pages, 7549 KB  
Article
Modulating Magnesium Ion Release for Dual Enhancement of Gel Properties and Nutrient Retention in Selenium-Enriched Tofu
by Fute Du, Tingting Tang, Jinxiaohan Zhang, Xiaoke Yan, Ying Xin, Yujie Su, Ming Zhang and Yuanqi Lv
Foods 2026, 15(3), 452; https://doi.org/10.3390/foods15030452 - 27 Jan 2026
Viewed by 574
Abstract
Traditional rapid coagulation processes often compromise the quality of selenium-enriched tofu, leading to suboptimal texture and substantial nutrient loss. This study regulated the gel properties and nutrient retention of selenium-enriched tofu by controlling magnesium ion (Mg2+) release from a water-in-oil (W/O) [...] Read more.
Traditional rapid coagulation processes often compromise the quality of selenium-enriched tofu, leading to suboptimal texture and substantial nutrient loss. This study regulated the gel properties and nutrient retention of selenium-enriched tofu by controlling magnesium ion (Mg2+) release from a water-in-oil (W/O) emulsion coagulant through shear rate adjustment (6000–12,000 r/min). The results demonstrated that at the optimal shear rate of 8000 r/min, sustained Mg2+ release facilitated the formation of a homogeneous and dense microstructure accompanied by significantly increased β-sheet content. Compared with conventional methods, the resulting tofu exhibited significant improvements in resilience (increased from 38.73% to 42.54%), water-holding capacity, and nutrient retention, with the selenium content rising from 44.42% to 54.57%. Conversely, deviations from this optimal condition produced either mechanically weak gels or structurally compromised networks with reduced nutrient retention capacity. This study establishes the regulation of shear rate to control Mg2+ release rate as an effective strategy for producing premium selenium-enriched tofu with synchronized optimization of texture and nutritional value, providing new insights for improving the overall quality of functional plant-based protein gels. Full article
(This article belongs to the Special Issue Effects of Processing on Protein Structure, Physicochemical Properties, and Function)
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23 pages, 5062 KB  
Article
Preparation, Characterization, and Mechanism of Hypoglycemic Action of a Goat Casein Peptide Delivery System Involving DPP-IV Inhibition and GLP-1 Release
by Xiaojing Du, Wenlin Niu and Hongxin Wang
Foods 2025, 14(21), 3795; https://doi.org/10.3390/foods14213795 - 5 Nov 2025
Cited by 1 | Viewed by 1406
Abstract
This study aimed to formulate a carrier system to improve the oral bioaccessibility of goat casein peptides (GCAPS). Goat casein was hydrolyzed with papain and subsequently purified to obtain bioactive peptide fractions (GCAPS) with potent hypoglycemic activity. On this basis, spherical GCAPS-loaded nanocarrier [...] Read more.
This study aimed to formulate a carrier system to improve the oral bioaccessibility of goat casein peptides (GCAPS). Goat casein was hydrolyzed with papain and subsequently purified to obtain bioactive peptide fractions (GCAPS) with potent hypoglycemic activity. On this basis, spherical GCAPS-loaded nanocarrier systems were developed, including liposomes (GCAPS-LS) and niosomes (GCAPS-NS). Among them, GCAPS-NS exhibited higher encapsulation efficiency (94.98 ± 3.01%) and a smaller particle size (89.81 ± 8.97 nm) than GCAPS-LS. FT-IR analysis confirmed successful peptide encapsulation. Simulated gastrointestinal digestion experiments demonstrated that GCAPS-NS significantly improved GCAPS retention and DPP-IV inhibition. In vivo results from high-fat diet-induced (HFD) insulin-resistant mice demonstrated that GCAPS-NS effectively ameliorated metabolic abnormalities by including adiposity, enhancing GLP-1 levels and suppressing hsCRP expression, thereby contributing to improved glycemic homeostasis. Moreover, GCAPS-NS intervention resulted in a significant enrichment of Akkermansia and a reduced Firmicutes/Bacteroidetes ratio, suggesting its beneficial role in alleviating HFD gut dysbiosis. These findings indicated that goat casein peptides held great potential as a functional food for the management of type 2 diabetes. Full article
(This article belongs to the Special Issue Effects of Processing on Protein Structure, Physicochemical Properties, and Function)
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