Effect of the Application of Novel Processes to Food Proteins on Structure, Physicochemical Properties and Modifications

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

Deadline for manuscript submissions: 31 August 2026 | Viewed by 2629

Special Issue Editors


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Guest Editor
SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China
Interests: preparation, digestion and absorption; functional evaluation of food-derived bioactive peptides; functional protein product development
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Guest Editor
SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China
Interests: protein development; functional protein; protein aggregation; interface regulation; thermal stability

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Guest Editor Assistant
SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China
Interests: protein modification; food hydrocolloids; functional protein product development; delivery system

Special Issue Information

Dear Colleagues,

With the rapid advancement of food science and technology, novel processing techniques (e.g., high-pressure processing, pulsed electric fields, ultrasound-assisted modification, enzymatic engineering, cold plasma treatment, and microwave irradiation) have garnered increasing attention in modulating food protein systems. These techniques enable the modulation of protein molecular conformations, functional group accessibility, and supramolecular aggregation states, consequently inducing significant alterations in their physicochemical properties (e.g., solubility, emulsifying capacity, gelation behavior, and thermal stability). Furthermore, these emerging techniques provide sustainable and efficient approaches for functionalizing proteins, advancing the development of protein-based functional foods with tailored nutritional and technological attributes.

We invite researchers to contribute their original research articles or review papers. Topics of interest include, but are not limited to, the following:

  • Novel processing techniques for food proteins, including physical, chemical, and enzymatic modifications;
  • Effects of processing methods on the structure and functional properties of food proteins;
  • Innovative application development of modified food proteins in functional foods;
  • Interactions of food proteins with other molecules in processing and their impact on food quality.

Dr. Shuzhen Cheng
Prof. Dr. Chao Wu
Guest Editors

Dr. Jianyu Zhu
Guest Editor Assistant

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Keywords

  • food protein
  • novel processing techniques
  • structure
  • physicochemical properties
  • modification
  • functional foods

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Published Papers (3 papers)

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Research

24 pages, 3294 KB  
Article
Ultrasound-Assisted Fibril Formation Enhances Complexation of Oat Globulin with Quercetin: Mechanism, Structure Evolution, Delivery Performance
by Jinzhao Xu, Xiao Zhao and Qingfeng Ban
Foods 2025, 14(22), 3916; https://doi.org/10.3390/foods14223916 - 16 Nov 2025
Viewed by 449
Abstract
Amyloid fibrillization represents an effective strategy for extending and enhancing protein function, particularly for the delivery of hydrophobic active substances. In this study, oat globulin (OG) and its fibrils were complexed with quercetin (Que) to construct the delivery system, and ultrasonic pretreatment was [...] Read more.
Amyloid fibrillization represents an effective strategy for extending and enhancing protein function, particularly for the delivery of hydrophobic active substances. In this study, oat globulin (OG) and its fibrils were complexed with quercetin (Que) to construct the delivery system, and ultrasonic pretreatment was applied during fibril preparation to explore the promoter of complex formation. The results demonstrated that complexation with Que induced a dose-dependent static quenching of the intrinsic fluorescence of the protein/fibrils, with hydrophobic interactions and tryptophan residues being the primary interaction forces and the main fluorescence quenching groups, respectively. In comparison, OG fibrils prepared with ultrasound pretreatment (UOGF) exhibited the strongest encapsulation and loading capacity for Que, ranging from 97.16% at a mass ratio of 200:1 to 42.48% at a ratio of 25:1. Subsequently, complexes were prepared with a ratio of 50:1. Structural analysis revealed that Que primarily interacts with the protein/fibril carriers through hydrogen bonds and hydrophobic interactions, inducing structural changes and ultimately being encapsulated in an amorphous form within the composite material. Additionally, Que promoted the mutual aggregation and cross-linking of protein/fibril units, leading to increased hydrodynamic diameter and zeta-potential. Moreover, UOGF-Que showed the greatest improvement in the thermal stability and the photostability of Que, and enhancing the bioaccessibility. These findings provide valuable insights into using ultrasound as an auxiliary measure for fibril self-assembly to enhance the application potential of fibrils, especially the delivery of hydrophobic functional substances. Full article
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20 pages, 7147 KB  
Article
Application Potential of Lion’s Mane Mushroom in Soy-Based Meat Analogues by High Moisture Extrusion: Physicochemical, Structural and Flavor Characteristics
by Yang Gao, Song Yan, Kaixin Chen, Qing Chen, Bo Li and Jialei Li
Foods 2025, 14(19), 3402; https://doi.org/10.3390/foods14193402 - 1 Oct 2025
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Abstract
The aim of this work was to systematically evaluate the effects of Lion’s Mane Mushroom powder (LMM, 0–40%) on the physicochemical properties, structural characteristics, and flavor profile of soy protein isolate-based high-moisture meat analogues (HMMAs). Optimal incorporation of 20% LMM significantly enhanced product [...] Read more.
The aim of this work was to systematically evaluate the effects of Lion’s Mane Mushroom powder (LMM, 0–40%) on the physicochemical properties, structural characteristics, and flavor profile of soy protein isolate-based high-moisture meat analogues (HMMAs). Optimal incorporation of 20% LMM significantly enhanced product quality by acting as a secondary phase that inhibited lateral protein aggregation while promoting longitudinal alignment, achieving a peak fibrous degree of 1.54 with dense, ordered fibers confirmed by scanning electron microscopy. Rheological analysis showed that LMM improved viscoelasticity (G′ > G″) through β-glucan; however, excessive addition (≥30%) compromised structural integrity due to insoluble dietary fiber disrupting protein network continuity, concurrently reducing thermal stability as denaturation enthalpy (ΔH) decreased from 1176.6 to 776.3 J/g. Flavor analysis identified 285 volatile compounds in HMMAs with 20% LMM, including 98 novel compounds, and 101 flavor metabolites were upregulated. The mushroom-characteristic compound 1-octen-3-ol exhibited a marked increase in its Relative Odor Activity Value of 18.04, intensifying mushroom notes. Furthermore, LMM polysaccharides promoted the Maillard reaction, increasing the browning index from 48.77 to 82.07, while β-glucan induced a transition in protein secondary structure from random coil to β-sheet configurations via intramolecular hydrogen bonding. In conclusion, 20% LMM incorporation synergistically improved texture, fibrous structure, and flavor complexity—particularly enhancing mushroom aroma. This research offers valuable insights and a foundation for future research for developing high-quality fungal protein-based meat analogues Full article
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17 pages, 3222 KB  
Article
Functionalization of Sodium Caseinate for Production of Neat Films: Effects of Casein Crosslinking Induced by Heating at Alkaline pH or Light Exposure
by Paolo D’Incecco, Stefano Gerna, Marta Sindaco, Luisa Pellegrino, Alberto Barbiroli, Veronica Rosi and Sara Limbo
Foods 2025, 14(16), 2764; https://doi.org/10.3390/foods14162764 - 8 Aug 2025
Viewed by 913
Abstract
This study explored the functionalization of sodium caseinate (NaCas) using environmentally friendly approaches to improve the mechanical and structural properties of the derived films. NaCas functionalization was achieved through casein crosslinking using two approaches: (i) thermal treatment at an alkaline pH to induce [...] Read more.
This study explored the functionalization of sodium caseinate (NaCas) using environmentally friendly approaches to improve the mechanical and structural properties of the derived films. NaCas functionalization was achieved through casein crosslinking using two approaches: (i) thermal treatment at an alkaline pH to induce the formation of lysinoalanine (LAL) and (ii) riboflavin-mediated photo-oxidation to induce the formation of di-tyrosine (di-Tyr). Starting from NaCas (not functionalized, control) obtained from pasteurized milk, three functionalized NaCas samples were prepared: one sample crosslinked by LAL, and two samples crosslinked by di-Tyr formed under LED light either with or without riboflavin. The amount of crosslinking was evaluated in the acid hydrolysates through HPLC methods using either fluorescence (di-Tyr) or MS (LAL) detection. Heat treatment at pH 9 induced the formation of up to 3540 µg of LAL/g casein, whereas LED light exposure in the presence of riboflavin promoted the formation of up to 500 µg of di-Tyr/g casein. The formation of crosslinks at the intermolecular level, which resulted in protein aggregation, was detected by SDS-PAGE. Films were obtained by mixing the water solutions of the four NaCas samples with glycerol as the plasticizer and casting them. The FTIR spectra revealed that the formation of crosslinks also induced changes in the secondary structure of NaCas, which were conserved in the derived films. Mechanical testing demonstrated that di-Tyr crosslinks enhanced film ductility, while LAL crosslinks increased tensile strength and stiffness. Full article
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