Application of Protein in Plant-Based Food: Processing, Function, and Health

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

Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 13921

Special Issue Editors


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Guest Editor
College of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: food; plant-based foods; proteins; food processing; conformation properties; functional properties; healthy benefits
College of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: soybean processing; structure and functional properties of protein; protein modification

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Co-Guest Editor
College of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: protein; fermented food; bioactive peptide; probiotics; biological activity
Special Issues, Collections and Topics in MDPI journals
College of Food Science, Northeast Agricultural University, Harbin 150030, China
Interests: nanoemulsion; protein; interactions of food compounds; vitamins

Special Issue Information

Dear Colleagues,

With the upgrading of consumers’ consumption concept and the rise in vegetarian culture, plant-based foods are expected to become the main trend in the food industry in the coming years. New products such as “vegetable meat”, “vegetable eggs”, and “vegetable milk” have entered the market in large numbers. A diversified plant-based food will contribute to the sustainable development of the environment system and enhance the diversity and stability of the food system. Proteins are significant food components. Due to their unique function properties, such as emulsification and gelation, they can show their performance in the processing of plant-based foods.

The goal of this Special Issue on “Application of Protein in Plant-Based Food: Processing, Function, and Health” is to invite authors to contribute original research articles as well as review articles focused on the development of plant-based foods, including their processing and modification, conformation and functional properties, and health benefits through the application of protein. It is our pleasure to invite you to submit to this Special Issue.

Best regards,

Prof. Dr. Yang Li
Dr. Baokun Qi
Dr. Shuang Zhang
Dr. Fei Teng
Guest Editors

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Keywords

  • plant-based foods
  • proteins
  • food processing
  • conformation properties
  • functional properties
  • healthy benefits

Published Papers (6 papers)

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Research

22 pages, 11074 KiB  
Article
Development of Plant-Based Adipose Tissue Analogs: Freeze-Thaw and Cooking Stability of High Internal Phase Emulsions and Gelled Emulsions
by Xiaoyan Hu and David Julian McClements
Foods 2022, 11(24), 3996; https://doi.org/10.3390/foods11243996 - 9 Dec 2022
Cited by 3 | Viewed by 2273
Abstract
There is great interest in the development of plant-based alternatives to meat products to meet the rising demand from vegans, vegetarians, and flexitarians. Ideally, these products should look, feel, taste, and behave like the meat products they are designed to replace. In this [...] Read more.
There is great interest in the development of plant-based alternatives to meat products to meet the rising demand from vegans, vegetarians, and flexitarians. Ideally, these products should look, feel, taste, and behave like the meat products they are designed to replace. In this study, we investigated the impact of simulated freeze–thaw and cooking treatments on the properties of plant-based adipose tissues formulated using high internal phase emulsions (HIPEs) or gelled emulsions (GEs). The HIPEs consisted of 75% oil, 2% soybean protein, 23% water, while the GEs consisted of 60% oil, 2% soybean protein, 2% agar and 36% of water. Low melting point (soybean oil) and high melting point (coconut oil) oils were used to create emulsions with either liquid or partially crystalline lipid phases at ambient temperature, respectively. In general, GEs were harder than HIPEs, and emulsions containing coconut oil were harder than those containing soybean oil at ambient temperatures. The thermal behavior of the plant-based adipose tissue was compared to that of beef adipose tissue. Beef adipose tissue was an opaque whitish semi-solid at ambient temperature. These properties could be mimicked with all types of HIPEs and GEs. The structure of the beef adipose tissue was resistant to freezing/thawing (−20/+20 °C) but not cooking (90 °C, 30 min). Soybean HIPEs and GEs were relatively stable to simulated cooking but not freeze–thawing. Conversely, coconut HIPEs and GEs exhibited the opposite behavior. These results have important implications for the formulation of alternatives to animal adipose tissue in plant-based foods. Full article
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13 pages, 2040 KiB  
Article
The Effect of Different Induction Methods on the Structure and Physicochemical Properties of Glycosylated Soybean Isolate Gels
by Jiangying Yu, Baozhong Sun, Songshan Zhang, Xiaochang Liu and Peng Xie
Foods 2022, 11(22), 3595; https://doi.org/10.3390/foods11223595 - 11 Nov 2022
Cited by 5 | Viewed by 1324
Abstract
Soybean protein isolate (SPI), as a full-valued protein, is rich in nutrients, such as amino acids. However, the isolated structure of soybeans makes it difficult to react and thus prepare good gels. In order to further improve the properties of SPIs and to [...] Read more.
Soybean protein isolate (SPI), as a full-valued protein, is rich in nutrients, such as amino acids. However, the isolated structure of soybeans makes it difficult to react and thus prepare good gels. In order to further improve the properties of SPIs and to prepare plant-based gels with good performance, this experiment was conducted to prepare maltodextrin glycosylated soybean isolate (MGSI) by the glycosylation of SPI and maltodextrin (MD), and the gels were prepared by thermal induction, transglutaminase (TGase) induction, and TG-MgCl2 co-induction of this glycosylated protein to investigate the effects of different induction methods on the structure and properties of the gels produced by MGSIs. Moreover, the effects of different induction methods on the structure and properties of the gels produced by MGSI were investigated. SDS-PAGE protein electrophoresis, FTIR spectroscopy, and endogenous fluorescence spectroscopy revealed that all three inductions result in the covalent bond cross-linking of MGSI during the gel formation process. Compared with thermal induction, the TGase-induced MGSI secondary structure had a higher content of β-folded structures, increased fluorescence intensity of tertiary structures, and produced a red shift. The gel induced by TGase in collaboration with MgCl2 contains a more β-folded structure and irregular curl and increases the β-turned angle and α-helix content further, the endogenous fluorescence λmax is significantly red-shifted, and the fluorescence intensity increases, demonstrating that the tertiary structure of MGSI unfolds the most, forming multilayered gels with the tightest structures. The three gels were analyzed by rheology and SEM, showing that the TGase-MgCl2 synergistically induced gel had the highest energy-storage modulus G’, viscoelasticity, and water-holding capacity, as well as the densest gel structure. In conclusion, the combined treatment of enzyme and MgCl2 might be an effective way of improving the structure and gel properties of SPI. This study helps to promote the high-value utilization of SPI and the development of plant protein gels. Full article
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10 pages, 2758 KiB  
Article
Effects of Bacillus subtilis BSNK-5-Fermented Soymilk on the Gut Microbiota by In Vitro Fecal Fermentation
by Yaxin Gao, Lizhen Hou, Miao Hu, Danfeng Li, Zhiliang Tian, Wei Wen, Bei Fan, Shuying Li and Fengzhong Wang
Foods 2022, 11(21), 3501; https://doi.org/10.3390/foods11213501 - 3 Nov 2022
Cited by 2 | Viewed by 1987
Abstract
The gut microbiota of soymilk intervention is beneficial to maintaining human health. Bacillus subtilis fermented soymilk has brought much interest, due to its richness of thrombolytic nattokinase and the strain of potential probiotic properties. In this study, soymilk was fermented by B. subtilis [...] Read more.
The gut microbiota of soymilk intervention is beneficial to maintaining human health. Bacillus subtilis fermented soymilk has brought much interest, due to its richness of thrombolytic nattokinase and the strain of potential probiotic properties. In this study, soymilk was fermented by B. subtilis BSNK-5, and the BSNK-5-fermented soymilk (SMF) on the production of short chain fatty acids (SCFAs) and the regulation of fecal microbiota was initially evaluated by in vitro fecal fermentation. SMF supplementation obviously increased the levels of SCFAs from 32.23 mM to 49.10 mM, especially acetic acid, propionic acid, and isobutyric acid. Additionally, SMF changed the composition and microbial diversity of gut microbiota. After 24 h of anaerobic incubation in vitro, SMF decreased the Firmicutes/Bacteroidota ratio favoring weight loss, increased Lachnospiraceae_UCG-004 and the other beneficial bacteria producing SCFAs, as well as suppressing pathogenic Streptococcus genus. These results revealed the potential use of BSNK-5-fermented soymilk as a potential candidate to promote gut health. Full article
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17 pages, 5899 KiB  
Article
Functionality of Pea-Grass Carp Co-Precipitated Dual-Protein as Affected by Extraction pH
by Xiaohu Zhou, Chaohua Zhang, Liangzhong Zhao, Wenhong Cao, Chunxia Zhou, Xin Xie and YuLian Chen
Foods 2022, 11(19), 3136; https://doi.org/10.3390/foods11193136 - 9 Oct 2022
Cited by 1 | Viewed by 1481
Abstract
Isoelectric solubilisation/co-precipitation (ISP) has been proven to be a better method than blending for preparing plant–animal dual-proteins, which can achieve synergies in the functional properties of heterologous proteins. This paper aims to investigate the effect of extraction pH on the functional properties of [...] Read more.
Isoelectric solubilisation/co-precipitation (ISP) has been proven to be a better method than blending for preparing plant–animal dual-proteins, which can achieve synergies in the functional properties of heterologous proteins. This paper aims to investigate the effect of extraction pH on the functional properties of co-precipitated dual-protein. The basic composition, subunit composition, solubility, surface hydrophobicity, emulsification and gel properties of co-precipitated dual-protein (Co) prepared from pea and grass carp with pH (2.0, 3.0, 9.0, 10.0 and 11.0) were analysed in this study using ISP. The results showed that the functional properties of Co (Co9, Co10, Co11) prepared by alkali extraction were generally better than those prepared by acid extraction (Co2, Co3). Among them, Co10 has the highest vicilin/legumin α + β value and solubility, while having the lowest surface hydrophobicity, making its emulsification and gel properties superior to other extraction pH values. This study provides an important method reference for preparing plant-animal Co with exceptional functional properties. Full article
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12 pages, 849 KiB  
Article
Effect of the Concentration, pH, and Ca2+ Ions on the Rheological Properties of Concentrate Proteins from Quinoa, Lentil, and Black Bean
by Julián Quintero, Juan D. Torres, Ligia Luz Corrales-Garcia, Gelmy Ciro, Efren Delgado and John Rojas
Foods 2022, 11(19), 3116; https://doi.org/10.3390/foods11193116 - 6 Oct 2022
Cited by 3 | Viewed by 1686
Abstract
Given consumer trends propelling a movement toward using plant protein in the food industry and searching for alternative protein ingredients by the industry, this study aimed to assess the influence of factors such as protein concentration, medium pH, and the presence of a [...] Read more.
Given consumer trends propelling a movement toward using plant protein in the food industry and searching for alternative protein ingredients by the industry, this study aimed to assess the influence of factors such as protein concentration, medium pH, and the presence of a divalent ion (Ca2+) upon the rheological properties such as viscosity change and gel formation of dispersion proteins extracted from quinoa, black beans, and lentils. A solution of each protein was prepared by varying its concentration (2.5%, 5.0%, and 10%), the pH (5.0, 7.0, and 9.0), and the incorporation of calcium chloride (0.0% and 1.0%). Each obtained solution was subjected to rheological tests to determine the parameters: consistency index (K), flow behavior (n), the storage (G’) and loss (G’’) modules, and the phase shift angle (δ). The results demonstrate that the incorporation of Ca2+, the shift in protein levels, and the decrease in pH modified the rheological behaviors of proteins, which were also influenced by the structural characteristics of each protein studied. However, thermal treatment and protein concentrations caused the most significant impact on proteins’ rheological behavior, forming gels independently of other conditions. It was possible to study and interpret the studied proteins’ rheological variations according to the environment’s conditions. Full article
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12 pages, 3355 KiB  
Article
Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut Protein
by Lingge Sun, Qingzhi Wu and Xiaoying Mao
Foods 2022, 11(16), 2432; https://doi.org/10.3390/foods11162432 - 12 Aug 2022
Cited by 16 | Viewed by 1838
Abstract
(1) Background: The effects of protein oxidization induced by malondialdehyde (MDA), which was selected as a representative of lipid peroxidation products, on the structure and functional properties of walnut protein were investigated. (2) Methods: Walnut protein isolate was produced by alkali-soluble acid precipitation. [...] Read more.
(1) Background: The effects of protein oxidization induced by malondialdehyde (MDA), which was selected as a representative of lipid peroxidation products, on the structure and functional properties of walnut protein were investigated. (2) Methods: Walnut protein isolate was produced by alkali-soluble acid precipitation. The modification of walnut protein isolate was conducted by MDA solutions (0, 0.01, 0.1, 1, and 10 Mm), which were incubated in the dark for 24 h. (3) Results: Increased carbonyl content and the degradation of sulfhydryl groups indicated MDA-induced protein oxidization. The circular dichroism spectra revealed disruption of the ordered protein secondary structure. The change in the tertiary conformation of the MDA-treated protein was observed through intrinsic fluorescence. Small polypeptide chain scission was observed at low MDA concentrations (≤0.1 mM) and protein aggregation was observed at high MDA concentrations (>0.1 mM) using high-performance size exclusion chromatography. Oxidized protein solubility was reduced. Furthermore, the emulsification stability index, foam capacity, and foam stability of walnut proteins were increased after treatment with 0.1 mM of MDA. An excessive concentration of MDA (>0.1 mM) decreased emulsification and foaming properties. (4) Conclusions: These results show that MDA oxidation modified the structure of walnut protein and further affected its function, which should be taken into account in processing walnut protein products. Full article
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