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A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Food Chemistry".

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 11793

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Special Issue Editors

Prof. Dr. Ti Li

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Guest Editor

College of Food Science and Technology, Nanchang University, Nanchang 330031, China
Interests: plant proteins; polyphenols; polysaccharides; interactions; nanoparticles; nutrition

Dr. Taotao Dai

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Guest Editor

Guangxi Key Laboratory of Fruits and Vegetables Storage-processing Technology, Guangxi Academy of Agricultural Sciences, Nanning 530007, China
Interests: plant proteins; plant-based emulsion; protein–polyphenol interaction; delivery systems; digestion
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Dear Colleagues,

Many food companies are replacing the animal-based proteins in their products, such as those derived from muscles, eggs, or milk, with plant-based ones. This trend is mainly driven by the perceived health and environmental benefits of plant-based proteins by consumers. As a natural macromolecule, plant protein can be used to prepare plant meat, plant-protein milk, plant-protein egg, plant-protein hydrogels, and so on. However, due to the limited solubility of plant proteins, many biological functions, such as emulsification and foaming, are limited. Thanks to the continuous efforts of scientists, many problems have been solved, and good plant-protein milks (Ripple Food) can be prepared. Therefore, this Special Issue focuses on the recent advances in plant-based proteins. We hope that the application and development of plant proteins can bring more healthy and delicious food to human beings.

Prof. Dr. Ti Li
Dr. Taotao Dai
Guest Editors

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Keywords

plant protein particles
plant protein-based emulsion
plant protein hydrogels
plant protein digestion
plant protein–nutrition interaction
plant protein complex

Published Papers (5 papers)

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Research

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15 pages, 1662 KiB

Open AccessArticle

Comparative Proteomics of Potato Cultivars with a Variable Dormancy Period

by Daniel Mouzo, Raquel Rodríguez-Vázquez, Carlos Barrio, Lucio García and Carlos Zapata

Molecules 2022, 27(19), 6621; https://doi.org/10.3390/molecules27196621 - 5 Oct 2022

Viewed by 1948

Abstract

The control of the duration of the dormancy phase is a significant challenge in the potato industry and for seed producers. However, the proteome landscape involved in the regulation of the length of the dormancy period over potato cultivars remains largely unexplored. In this study, we performed for the first time a comparative proteome profiling of potato cultivars with differential duration of tuber dormancy. More specifically, the proteome profiling of Agata, Kennebec and Agria commercial potato varieties with short, medium and medium-long dormancy, respectively, was assessed at the endodormancy stage using high-resolution two-dimensional electrophoresis (2-DE) coupled to reversed-phase liquid chromatography–tandem mass spectrometry (LC-TripleTOF MS/MS). A total of 11 proteins/isoforms with statistically significant differential abundance among cultivars were detected on 2-DE gels and confidently identified by LC-TripleTOF MS/MS. Identified proteins have known functions related to tuber development, sprouting and the oxylipins biosynthesis pathway. Fructokinase, a mitochondrial ADP/ATP carrier, catalase isozyme 2 and heat shock 70 kDa were the proteins with the strongest response to dormancy variations. To the best of our knowledge, this study reports the first candidate proteins underlying variable dormancy length in potato cultivars. Full article

(This article belongs to the Special Issue Recent Advances in Plant-Based Proteins)

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14 pages, 1953 KiB

Open AccessArticle

Comparison on Protein Bioaccessibility of Soymilk Gels Induced by Glucono-δ-Lactone and Lactic Acid Bacteria

by Tianran Hui, Ting Tang, Xuan Gu, Zhen Yuan and Guangliang Xing

Molecules 2022, 27(19), 6202; https://doi.org/10.3390/molecules27196202 - 21 Sep 2022

Cited by 2 | Viewed by 1895

Abstract

In this study, the protein bioaccessibility of soymilk gels produced by the addition of glu-cono-δ-lactone (GDL) and fermentation with lactic acid bacteria (LAB) was examined using an in vitro gastrointestinal simulated digestion model. The in vitro protein digestibility, soluble protein content, free amino acids contents, degree of hydrolysis, electrophoretic patterns, and peptide content were measured. The results suggested that acid-induced soymilk gel generated by GDL (SG) showed considerably reduced in vitro protein digestibility of 75.33 ± 1.00% compared to the soymilk gel induced by LAB (SL) of 80.57 ± 1.53% (p < 0.05). During the gastric digestion stage, dramatically higher (p < 0.05) soluble protein contents were observed in the SG (4.79–5.05 mg/mL) than that of SL (4.31–4.35 mg/mL). However, during the later intestinal digestion phase, the results were the opposite. At the end of the gastrointestinal digestion phase, the content of small peptides was not significantly different (p > 0.05) between the SL (2.15 ± 0.03 mg/mL) and SG (2.17 ± 0.01 mg/mL), but SL showed higher content of free amino acids (20.637 g/L) than that of SG (19.851 g/L). In general, soymilk gel induced by LAB had a higher protein bioaccessibility than the soymilk gel coagulated by GDL. Full article

(This article belongs to the Special Issue Recent Advances in Plant-Based Proteins)

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17 pages, 3578 KiB

Open AccessArticle

Gel Property of Soy Protein Emulsion Gel: Impact of Combined Microwave Pretreatment and Covalent Binding of Polyphenols by Alkaline Method

by Jing Xu, Fei Teng, Baiqi Wang, Xinxuan Ruan, Yifan Ma, Dingyuan Zhang, Yan Zhang, Zhijun Fan and Hua Jin

Molecules 2022, 27(11), 3458; https://doi.org/10.3390/molecules27113458 - 27 May 2022

Cited by 14 | Viewed by 2202

Abstract

This study investigated the effects of microwave modification, alkali polyphenol (ferulic acid) covalently combined modification, and microwave-alkali polyphenol covalently combined modification on the gel properties of soy protein emulsions. The results showed that the properties of soy protein emulsions were improved significantly by the three modification methods. After three kinds of modification, the viscoelasticity of soy protein emulsion gel increased, and a gel system with stronger elasticity was formed. The texture, water-holding, and hydration properties of the emulsion gel increased significantly. The SEM and ClSM results showed that the modified soy protein emulsion gel had a more compact and uniform porous structure, and the oil droplets could be better embedded in the network structure of the gel. Among the three modification methods, the microwave-alkali method polyphenol covalently combining the compound modification effect was best, and the microwave modification effect was least effective compared to the other two methods. Our obtained results suggested that for gel property modification of soy protein emulsion gels, microwave pretreatment combined with the covalent binding of polyphenols by an alkaline method is an effective method. Full article

(This article belongs to the Special Issue Recent Advances in Plant-Based Proteins)

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19 pages, 2727 KiB

Open AccessArticle

The Effect of Precipitation pH on Protein Recovery Yield and Emulsifying Properties in the Extraction of Protein from Cold-Pressed Rapeseed Press Cake

by Cecilia Ahlström, Johan Thuvander, Marilyn Rayner, María Matos, Gemma Gutiérrez and Karolina Östbring

Molecules 2022, 27(9), 2957; https://doi.org/10.3390/molecules27092957 - 5 May 2022

Cited by 5 | Viewed by 1969

Abstract

Rapeseed is the second most cultivated oilseed after soybean and is mainly used to produce vegetable oil. The by-product rapeseed press cake is rich in high-quality proteins, thus having the possibility of becoming a new plant protein food source. This study aimed to investigate how the precipitation pH affects the protein yield, protein content, and emulsifying properties when industrially cold-pressed rapeseed press cake is used as the starting material. Proteins were extracted under alkaline conditions (pH 10.5) with an extraction coefficient of 52 ± 2% followed by precipitation at various pH (3.0–6.5). The most preferred condition in terms of process efficiency was pH 4.0, which is reflected in the zeta potential results, where the proteins’ net charge was 0 at pH 4.2. pH 4.0 also exhibited the highest protein recovery yield (33 ± 0%) and the highest protein concentration (64 ± 1%, dry basis). Proteins precipitated at pH 6.0–6.5 stabilized emulsions with the smallest initial droplet size, although emulsions stabilized by rapeseed protein precipitated at pH 5.0–6.0 showed the highest emulsion stability at 37 °C for 21 days, with a limited layer of free oil. Overall, emulsion stabilized by protein precipitated at pH 5.0 was the most stable formulation, with no layer of free oil after 21 days of incubation. Full article

(This article belongs to the Special Issue Recent Advances in Plant-Based Proteins)

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Review

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24 pages, 936 KiB

Open AccessReview

High-Moisture Shear Processes: Molecular Changes of Wheat Gluten and Potential Plant-Based Proteins for Its Replacement

by Nicola Gasparre, Marco van den Berg, Filip Oosterlinck and Arjen Sein

Molecules 2022, 27(18), 5855; https://doi.org/10.3390/molecules27185855 - 9 Sep 2022

Cited by 10 | Viewed by 2822

Abstract

Nowadays, a growing offering of plant-based meat alternatives is available in the food market. Technologically, these products are produced through high-moisture shear technology. Process settings and material composition have a significant impact on the physicochemical characteristics of the final products. Throughout the process, the unfolded protein chains may be reduced, or associate in larger structures, creating rearrangement and cross-linking during the cooling stage. Generally, soy and pea proteins are the most used ingredients in plant-based meat analogues. Nevertheless, these proteins have shown poorer results with respect to the typical fibrousness and juiciness found in real meat. To address this limitation, wheat gluten is often incorporated into the formulations. This literature review highlights the key role of wheat gluten in creating products with higher anisotropy. The generation of new disulfide bonds after the addition of wheat gluten is critical to achieve the sought-after fibrous texture, whereas its incompatibility with the other protein phase present in the system is critical for the structuring process. However, allergenicity problems related to wheat gluten require alternatives, hence an evaluation of underutilized plant-based proteins has been carried out to identify those that potentially can imitate wheat gluten behavior during high-moisture shear processing. Full article

(This article belongs to the Special Issue Recent Advances in Plant-Based Proteins)

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