Plant Protein Processing: Technological Innovation and New Application Scenarios

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

Deadline for manuscript submissions: 30 May 2025 | Viewed by 4492

Special Issue Editors


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Guest Editor
College of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: egetable protein; structural characterization; emulsifying activity; interfacial activity; gel property; physical field regulation
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
College of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: food protein; protein structure; food flavor; protein function; emulsion

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Guest Editor Assistant
School of Food Science and Engineering, Hainan University, Haikou 570228, China
Interests: vegetable protein; structural lipids; oxidation; emulsifying activity; oil safety; functionality

Special Issue Information

Dear Colleagues,

Plant protein, as a high-quality protein resource, has great potential for development and plays an important role in meeting people's demand for food protein. The rapid development of plant-based milk and plant-based meat has formed a stable market. Through technological innovation, the utilization level of traditional food has been improved. This achieves the improvement in the nutritional value and functional characteristics of plant proteins and develops the categories belonging to the characteristic flavor of plant protein itself. Obviously, the full development of proteins with high nutritional value and functional properties through technological innovation can promote the application of plant proteins in new scenarios.

Therefore, this Special Issue aims to present recent advances in technological innovation and applications in plant protein processing. We encourage the submission of manuscripts that include, but are not limited to, the following topics:

  • Innovation and utilization of plant protein in plant-based foods;
  • Processing and utilization pathways of plant protein resources;
  • Efficient utilization pathways of plant protein resources;
  • Technological innovation in plant protein processing;
  • Mechanisms of plant protein processing to improve nutritional value and functional properties;
  • Relationship between plant protein processing and protein flavor;
  • Development of plant-based products with high added value, high nutrition, and high efficiency;
  • Application of plant protein in formula food for special medical purposes.

Prof. Dr. Zhongjiang Wang
Dr. Zengwang Guo
Guest Editors

Dr. Zhaoxian Huang
Guest Editor Assistant

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Keywords

  • plant protein
  • processing technology
  • technological innovation
  • new scenario applications
  • innovation and utilization
  • plant-based foods
  • product development

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Published Papers (4 papers)

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Research

23 pages, 3617 KiB  
Article
Exploration of Pea Protein Isolate–Sodium Alginate Complexes as a Novel Strategy to Substitute Sugar in Plant Cream: Synergistic Interactions Between the Two at the Interface
by Jingru Sun, Xiyuan Yang, Jingjing Diao, Yichang Wang and Changyuan Wang
Foods 2025, 14(6), 991; https://doi.org/10.3390/foods14060991 - 14 Mar 2025
Viewed by 577
Abstract
This study aims to explore the feasibility of using pea protein isolate (PPI)/sodium alginate (SA) complex as a sugar substitute to develop low sugar plant fat cream. Firstly, this study analyzed the influence of SA on the structure and physicochemical properties of PPI [...] Read more.
This study aims to explore the feasibility of using pea protein isolate (PPI)/sodium alginate (SA) complex as a sugar substitute to develop low sugar plant fat cream. Firstly, this study analyzed the influence of SA on the structure and physicochemical properties of PPI and evaluated the types of interaction forces between PPI and SA. The addition of SA effectively induces the unfolding and structural rearrangement of PPI, causing structural changes and subunit dissociation of PPI, resulting in the exposure of internal-SH groups. In addition, the addition of SA increased the content of β-folding in PPI, making the structure of PPI more flexible and reducing interfacial tension. The ITC results indicate that the binding between PPI and SA exhibits characteristics of rapid binding and slow dissociation, which is spontaneous and accompanied by heat release. Next, the effect of PPI/SA ratio on the whipping performance and quality of low sugar plant fat creams was studied by using PPI/SA complex instead of 20% sugar in the cream. When using a PPI/SA complex with a mass ratio of 1:0.3 instead of sugar, the stirring performance, texture, and stability of plant fat cream reach their optimum. Finally, the relevant analysis results indicate that the flexibility and interface characteristics of PPI are key factors affecting the quality of cream. This study can provide theoretical support for finding suitable sugar substitute products and developing low sugar plant fat cream. Full article
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25 pages, 5732 KiB  
Article
Synergistic Effects of Ultrasound and pH-Shifting on the Solubility and Emulsification Properties of Peanut Protein
by Zhuoran Jiao, Zhiqiang Feng, Siqi Zhao, Yuwei Wang, Miao Feng, Qian Chen, Baohua Kong and Haotian Liu
Foods 2025, 14(5), 853; https://doi.org/10.3390/foods14050853 - 2 Mar 2025
Viewed by 734
Abstract
Peanut protein is a byproduct of peanut oil extraction with limited applications within the food sector due to its low solubility and emulsifying properties. This study investigated the influences and mechanisms of high-intensity ultrasound (HIU, 200~600 W) and pH-shifting (pH 12), either individually [...] Read more.
Peanut protein is a byproduct of peanut oil extraction with limited applications within the food sector due to its low solubility and emulsifying properties. This study investigated the influences and mechanisms of high-intensity ultrasound (HIU, 200~600 W) and pH-shifting (pH 12), either individually or jointly, on the structure, solubility, and emulsifying properties of PP. Results indicated that the solubility of PP significantly increased after the combined treatment, particularly when the HIU power was 300 W (p < 0.05). Accordingly, emulsions prepared from it exhibited highest storage stability. Structural analysis indicated that the increased PP solubility (9.95% to 54.37%, p < 0.05) is mainly attributed to the structural changes that occur during protein unfolding, resulting in the uncovering of hydrophobic groups (7181.43 to 14,083.00, p < 0.05) and the reduction of α-helices (24.43% to 18.17%, p < 0.05). Moreover, confocal laser scanning microscopy of the emulsions revealed that the combination-treated PP resulted in smaller protein particle sizes (50.09 μm to 15.68 μm, p < 0.05), tighter adsorption on the oil–water interface, and a denser and more stable interfacial film compared to the native and the individual treatment, thereby enhancing the stability of the system. A rheological analysis confirmed that the combined treatment improved the interfacial properties of the protein, which was advantageous for emulsion stability. In conclusion, HIU combined with pH12-shifting can appreciably improve the solubility and emulsifying properties of PP to broaden its application prospects. Full article
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17 pages, 2757 KiB  
Article
Betalain–Chickpea Protein Particles Produced by Freeze Drying and Spray Drying: Physicochemical Aspects, Storage Stability, and In Vitro Digestion
by Mary H. Grace, Roberta Targino Hoskin, Malak Alghamdi, Mary Ann Lila and Vesela I. Chalova
Foods 2025, 14(2), 281; https://doi.org/10.3390/foods14020281 - 16 Jan 2025
Viewed by 1159
Abstract
Beetroots are one of the primary sources of betalains, nitrogenous pigments with anti-inflammatory and antioxidant properties. However, due to their chemical instability, betalains have limited use in food applications. This work investigated whether betalains encapsulated in chickpea protein could be stabilized and delivered [...] Read more.
Beetroots are one of the primary sources of betalains, nitrogenous pigments with anti-inflammatory and antioxidant properties. However, due to their chemical instability, betalains have limited use in food applications. This work investigated whether betalains encapsulated in chickpea protein could be stabilized and delivered in a shelf-stable format. Freeze-dried (CB-FD) and spray-dried (CB-SD) protein–betalain particles encapsulated in chickpea protein isolate (6% w/v) were prepared. The encapsulation method affected particles’ morphology, water activity, hygroscopicity, solubility, and color. Particles captured total betalains of 9.30 ± 0.61 and 4.40 ± 0.92 mg/g for CB-SD and CB-FD, respectively. LC-MS identified 12 betacyanins and 6 betaxanthins. The stability of betalains revealed that encapsulation efficiently preserved betalain integrity of over 6 weeks of storage at 4, 22, and 40 °C compared to dry beetroot extract. CB-SD particles were stable with no significant changes, while CB-FD showed slight degradation after 4 weeks due to increased Aw. Antioxidant activity correlated well with betalain concentration. In vitro digestion resulted in only 25% bioaccessibility of betacyanins, while betaxanthins were more stable with 100% recovery. Encapsulation with chickpea protein isolate is an efficient and straightforward strategy for expanding and diversifying applications of phytochemical-rich beetroot extracts for the food industry. Full article
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13 pages, 2638 KiB  
Article
Effect of Pea Protein Isolate–Soybean Meal Ratio on Fiber Structure and Texture Properties of High-Moisture Meat Analogs
by Zhongjiang Wang, Yachao Tian, Fangxiao Lou and Zengwang Guo
Foods 2024, 13(23), 3818; https://doi.org/10.3390/foods13233818 - 27 Nov 2024
Cited by 1 | Viewed by 1408
Abstract
Inadequate fibrous attributes and prohibitive pricing are pivotal barriers to the broader market penetration of meat analogs (MAs). This research endeavors to address these impediments by formulating a blend of cost-effective soybean meal (SM) and pea protein isolate (PPI) across a spectrum of [...] Read more.
Inadequate fibrous attributes and prohibitive pricing are pivotal barriers to the broader market penetration of meat analogs (MAs). This research endeavors to address these impediments by formulating a blend of cost-effective soybean meal (SM) and pea protein isolate (PPI) across a spectrum of ratios (PPI:SM = 1:0, 8:2, 6:4, 4:6, 2:8, and 0:1). The analysis of textural properties elucidated that the integration of SM markedly diminished the textural rigidity and mastication resistance of MAs. Employing scanning electron microscopy (SEM) and fibrillation degree metrics, it was ascertained that the most favorable fibrous architecture of MAs was attained at a PPI to SM ratio of 6:4. Further experimental evidence underscored that the synergistic interaction between SM and PPI catalyzed the conversion of free sulfhydryl groups into disulfide linkages, a pivotal mechanism in the augmentation of MAs’ fibrous matrices. The conclusions drawn from this study provide substantive contributions to the formulation of superior-quality, economically viable MAs, and could potentially accelerate their market acceptance. Full article
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