Advanced Technology to Improve Plant Protein Functionality

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

Deadline for manuscript submissions: 31 July 2025 | Viewed by 1163

Special Issue Editors


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Guest Editor
College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety, Nanjing University of Finance and Economics, Nanjing 210023, China
Interests: technical functionality (solubility, emulsification, foaming, gelation) of cereal proteins; physicochemical properties of proteins; structure–function relationships of proteins; protein–polysaccharide interactions

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Guest Editor
College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety, Nanjing University of Finance and Economics, Nanjing 210023, China
Interests: structure and quality regulation of plant protein-based emulsions; new healthy plant-based products; high-value utilization of grain by-products

Special Issue Information

Dear Colleagues,

Proteins are important macronutrients for humans; traditionally, animal proteins (mainly including meat, eggs, and milk) have been the main source of dietary protein. However, as the global population is projected to increase to 9.5 billion by 2050, this will result in a 30–50% increase in protein demand. Considering the fact that the production of these animal proteins is largely dependent on plant-based feeds, the conversion of plant proteins into these animal proteins is only about 3% efficient. It also leads to more greenhouse gas emissions, the consumption of more water and the use of land. In addition, human health concerns, animal welfare, and religion are also topics for consideration. A combination of these factors has led to a growing demand for plant proteins to replace animal proteins in recent years. However, since plant proteins are usually obtained from agricultural by-products or require more complex extraction procedures, their technical functionality (solubility, emulsification, foaming, gelation, etc.) is much weaker than animal proteins. Therefore, there is an urgent need to explore new and advanced technologies to enhance the functional properties of plant proteins as effective alternatives to animal proteins.

Dr. Wenfei Xiong
Dr. Jian Ding
Guest Editors

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Keywords

  • cereal protein
  • gelation
  • emulsifying
  • foaming
  • interactions
  • oilseed protein
  • structure
  • physical modification
  • chemical modification
  • bio-modification
  • extraction and separation

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Published Papers (2 papers)

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Research

17 pages, 13054 KiB  
Article
Effect of pH-Shifted Compound Heating Treatment on the Structure and Properties of Walnut Protein Isolate
by Liwen Chai, Wei Shi, Yunxia Tan, Xudong Che, Jiankang Lu, Bingyao Bai and Chunlan Zhang
Foods 2025, 14(10), 1754; https://doi.org/10.3390/foods14101754 - 15 May 2025
Viewed by 320
Abstract
This study aims to explore the effect of pH on the solubility of walnut protein isolate (WPI) across a pH range of 7.0 to 12.0. The findings reveal that WPI solubility increased with rising pH levels, reaching a maximum solubility of 61.13% (4.79 [...] Read more.
This study aims to explore the effect of pH on the solubility of walnut protein isolate (WPI) across a pH range of 7.0 to 12.0. The findings reveal that WPI solubility increased with rising pH levels, reaching a maximum solubility of 61.13% (4.79 mg/mL) at pH 12.0. Building on these results, WPI was subjected to compound heating at pH 12.0, with temperatures ranging from 60 °C to 100 °C (maintained for 30 min), to evaluate its structural and functional properties. Compared to the control group, WPI solubility peaked at 80.56% when heated to 90 °C. Additionally, its foaming capacity rose to 118.22% ± 7.34, accompanied by improved foaming stability. The average particle size decreased to 151.93 nm, while the surface charge increased to −28.33 mV. The protein subunits progressively aggregated within the range of 20.0 kDa to 14.1 kDa, and the surface hydrophobicity decreased. Scanning electron microscopy revealed that the surface morphology of the WPI became increasingly smooth with rising heating temperatures. Moreover, significant changes were observed in the secondary structure of the WPI. This study underscores the potential of pH-shifted compound heating treatment as a promising processing technique for WPI, offering key insights into the optimization of walnut protein processing. Full article
(This article belongs to the Special Issue Advanced Technology to Improve Plant Protein Functionality)
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15 pages, 4829 KiB  
Article
Physicochemical Properties of Moderately Heat-Treated Rice Protein Within Alkaline Solution and Its Evaluation as a Spray-Drying Microencapsulation Wall Material
by Mengqi Liu, Rumeng Huang, Lifeng Wang, Mohamed Eid and Wenfei Xiong
Foods 2025, 14(10), 1739; https://doi.org/10.3390/foods14101739 - 14 May 2025
Viewed by 345
Abstract
This study addresses the shortcoming of rice protein, which has limited its widespread use as a food ingredient due to its extremely low solubility in neutral aqueous solution. Herein, rice protein (RP) was dispersed in aqueous solutions with different alkali concentrations (0.075 M~0.125 [...] Read more.
This study addresses the shortcoming of rice protein, which has limited its widespread use as a food ingredient due to its extremely low solubility in neutral aqueous solution. Herein, rice protein (RP) was dispersed in aqueous solutions with different alkali concentrations (0.075 M~0.125 M), and then heat-treated (80 °C, 1~4 h) to obtain a modified RP. The physicochemical properties of the modified RP in neutral aqueous solution and its performance as a microencapsulated wall material were then comprehensively analyzed. The results showed that the solubility of the RP at pH 7.0 could be increased to more than 56.3% by alkali solution combined with moderate heat treatment for 1 h. Further analysis revealed that the enhancement of the RP solubility performance was mainly due to the depolymerization of rice glutenin cluster aggregates, with the average size decreasing to 140~180 nm, which was also accompanied by an increase in net zeta potential. Structural analysis pointed to a significant decrease in the surface hydrophobicity and free sulfhydryl content of the RP after thermal treatment in alkaline solution, while degradation of glutenin subunits (especially for the results of alkaline treatment at higher concentrations) and an increase in random coil content occurred. These physicochemical properties and conformational transitions of the modified RP contributed to its excellent emulsification properties and microencapsulation ability (encapsulation efficiency > 97%). Nevertheless, the redispersing properties of microcapsules prepared with the modified RP as a wall material were significantly weaker than those of sodium caseinate. These findings provide new guidance and insights into the modulation of functional properties and applications of RP. Full article
(This article belongs to the Special Issue Advanced Technology to Improve Plant Protein Functionality)
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