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Sustainable Protein Sources: Extraction, Structural Characterization, and Functional Properties
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Sustainable Protein Sources: Extraction, Structural Characterization, and Functional Properties

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 November 2025 | Viewed by 5568

Special Issue Editors

Dr. Armin Mirzapour-Kouhdasht

E-Mail Website
Guest Editor
Department of Food Science, Purdue University, West Lafayette, IN 47907, USA
Interests: proteins and peptides; bioactive compounds; enzyme inhibition assays; functional foods; protein digestibility and bioavailability
Special Issues, Collections and Topics in MDPI journals
Dr. Jen-Yi Huang

E-Mail Website
Guest Editor
Department of Food Science, Purdue University, West Lafayette, IN 47907, USA
Interests: sustainable food systems; life cycle assessment of food; cold plasma processing; electrodialysis membrane filtration
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

From the perspective of higher global demand for protein, it has been of crucial importance to look into sustainable and other alternative protein sources that may offer food security with minimal environmental impacts. This Special Issue, entitled "Sustainable Protein Sources: Extraction, Structural Characterization, and Functional Properties", invites research and review articles that address innovative approaches to the extraction, structural characterization, and functional evaluation of proteins obtained from sustainable sources, such as algae, insects, pulses, cereals, and other plant-based materials. Of particular interest are studies that contribute to the understanding of such proteins' structure–function relationship and their applications in food systems. Original contributions dealing with novel technologies and the impact of processing on improving protein functionality, digestibility, and bioavailability while reducing their allergenicity and toxicity are also welcome. Contributions on the role of protein in food formulation, 3D printing, and the elaboration of functional foods are invited. We aim to assemble a collection of state-of-the-art knowledge to drive the expanding application of food products derived from sustainable protein sources in food science and technology.

We look forward to your valuable contributions.

Dr. Armin Mirzapour-Kouhdasht
Dr. Jen-Yi Huang
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • protein
  • plant-based
  • algae
  • pulses
  • cereals
  • insects
  • functionality
  • structure–function relationship
  • digestibility and bioavailability
  • allergenicity and toxicity

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Published Papers (4 papers)

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Research

21 pages, 3820 KiB  
Article
Anti-Diabetic Effect of Soy–Whey Dual-Protein on Mice with Type 2 Diabetes Mellitus Through INS/IRS1/PI3K Signaling Pathway
by Na Li, Hu Li, Duo Feng, Mengjie Li, Di Han, Tianxin Liu and Jing Wang
Foods 2025, 14(12), 2115; https://doi.org/10.3390/foods14122115 - 16 Jun 2025
Viewed by 399
Abstract
The effects of soy protein and whey protein supplementation on glycemic control show inconsistency, and the mechanisms underlying the impact of a high-protein diet on blood glucose regulation remain unclear. This study aimed to explore the impact of a dual-protein (DP) blend comprising [...] Read more.
The effects of soy protein and whey protein supplementation on glycemic control show inconsistency, and the mechanisms underlying the impact of a high-protein diet on blood glucose regulation remain unclear. This study aimed to explore the impact of a dual-protein (DP) blend comprising soy protein isolate (SPI) and whey protein concentrate (WPC), processed through high-pressure homogenization, on mice with Type 2 diabetes mellitus (T2DM) and its potential mechanisms. In the in vitro experiments, an insulin-resistant (IR) HepG2 cell model was treated with DP, resulting in a significant enhancement of glucose uptake and upregulation of IRS1 and GLUT4 expression. For the in vivo experiments, male C57BL/6J mice were randomly assigned into four groups (n = 6) based on body weight: normal control, T2DM model group, Metformin-treated group, and DP-treated group. Following a 5-week feeding period, Metformin and DP significantly reduced levels of blood sugar, AUC, TC, TG, and LDL-C in T2DM mice. Additionally, TP and ALB levels in the DP group were notably higher in the model group. In the liver and pancreas, DP alleviated histopathological changes and promoted liver glycogen synthesis in T2DM mice. Moreover, the levels of IRS1 and PI3K in the livers of mice in the DP group were significantly higher than those in the model group. Compared with the model groups, DP significantly reduced the expression of CD45 and increased the expression of CD206 in the pancreas of mice. Furthermore, 16S rRNA analysis revealed that DP altered the composition of the gut microbiota in diabetic mice, increasing the relative abundance of Lactobacillus, Parvibacter, and Lactobacillaceae. This suggested that DP could alleviate functional metabolic disorders in the gut and potentially reverse the risk of related complications. In conclusion, soy whey dual-protein may have an effective nutritional therapeutic effect on T2DM mice by regulating lipid metabolism, the INS/IRS1/PI3K signaling pathway, and gut microbiota. Full article
(This article belongs to the Special Issue Sustainable Protein Sources: Extraction, Structural Characterization, and Functional Properties)
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24 pages, 12128 KiB  
Article
Effects of Conjugation with Basil Seed Gum on Physicochemical, Functional, Foaming, and Emulsifying Properties of Albumin, Whey Protein Isolate and Soy Protein Isolate
by Hadi Hashemi, Mohammad Hadi Eskandari, Mohammadreza Khalesi, Mohammad-Taghi Golmakani, Mehrdad Niakousari and Seyed Mohammad Hashem Hosseini
Foods 2025, 14(3), 390; https://doi.org/10.3390/foods14030390 - 24 Jan 2025
Viewed by 1002
Abstract
Protein conjugation with the Maillard reaction has received considerable attention in the past decades in terms of improving functional properties. This study evaluated the changes in the techno-functional properties of whey protein isolate (WPI), soy protein isolate (SPI), and albumin (Alb) after conjugation [...] Read more.
Protein conjugation with the Maillard reaction has received considerable attention in the past decades in terms of improving functional properties. This study evaluated the changes in the techno-functional properties of whey protein isolate (WPI), soy protein isolate (SPI), and albumin (Alb) after conjugation with basil seed gum (BSG). The conjugates were developed via the Maillard reaction. Various analyses including FT-IR, XRD, SEM, SDS-PAGE, DSC, RVA, rheology, zeta potential, emulsion, and foaming ability were used for evaluating conjugation products. Conjugation between proteins (WPI, SPI, Alb) and BSG was validated by FT-IR spectroscopy. XRD results revealed a decrease in the peak of BSG after conjugation with proteins. SDS-PAGE demonstrated the conjugation of WPI, SPI, and Alb with BSG. DSC results showed that conjugation with BSG reduced the Tg of WPI, SPI, and Alb from 210.21, 207.21, and 210.90 °C to 190.30, 192.91, and 196.66 °C, respectively. The emulsion activity and emulsion stability of protein/BSG conjugates were increased significantly. The droplet size of emulsion samples ranged from 112.1 to 239.3 nm on day 3. Nanoemulsions stabilized by Alb/BSG conjugate had the smallest droplet sizes (112.1 and 143.3 nm after 3 and 17 days, respectively). The foaming capacity of WPI (78.57%), SPI (61.91%), and Alb (71.43%) in their mixtures with BSG increased to 107.14%, 85.71%, and 85.71%, respectively, after making conjugates with BSG. The foam stability of WPI (39.34%), SPI (61.57%), and Alb (53.37%) in their mixtures with BSG (non-conjugated condition) increased to 77.86%, 77.91%, and 72.32%, respectively, after formation of conjugates with BSG. Conjugation of BSG to proteins can improve the BSG applications as a multifunctional stabilizer in pharmaceutical and food industries. Full article
(This article belongs to the Special Issue Sustainable Protein Sources: Extraction, Structural Characterization, and Functional Properties)
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21 pages, 1912 KiB  
Article
Unravelling the Digestibility and Structure–Function Relationship of Lentil Protein Through Germination and Molecular Weight Fractionation
by Armin Mirzapour-Kouhdasht, Samaneh Shaghaghian, Marjan Majdinasab, Jen-Yi Huang and Marco Garcia-Vaquero
Foods 2025, 14(2), 272; https://doi.org/10.3390/foods14020272 - 16 Jan 2025
Viewed by 1480
Abstract
This study explores for the first time the impact of a 6-day germination process on the structure (FTIR), antioxidant activity, nutritional/safety attributes (ACE-I inhibitory activity, digestibility, and cytotoxicity), and functional properties of fractions of variable molecular weight (W > 5 kDa; 3 kDa [...] Read more.
This study explores for the first time the impact of a 6-day germination process on the structure (FTIR), antioxidant activity, nutritional/safety attributes (ACE-I inhibitory activity, digestibility, and cytotoxicity), and functional properties of fractions of variable molecular weight (W > 5 kDa; 3 kDa < MW < 5 kDa; and MW < 3 kDa) isolated from proteins extracted from lentils. FTIR results indicated a substantial increase in β-sheet contents during germination. The digestibility of proteins increased from day 0 (16.32–17.04%) to day 6 of germination (24.92–26.05%) with variable levels of digestibility depending on their MW. ACE-I inhibitory activity improved during germination in all fractions, reaching IC50 values of 0.95, 0.83, and 0.69 mg/mL after 6 days of germination. All antioxidant activities analyzed notably increased, particularly in low-MW fractions (MW < 3 kDa). The functional properties of low-MW fractions were also the most promising, displaying the highest water and fat binding capacities and emulsifying and foaming capacities but lower foaming and emulsifying stability compared to high-MW fractions. Cytotoxicity tests on L929 cells revealed the slight adverse effects of low-MW fractions during germination. This study provides insights into the enhanced nutritional and functional attributes of lentil proteins following germination, emphasizing their potential application in functional foods. Full article
(This article belongs to the Special Issue Sustainable Protein Sources: Extraction, Structural Characterization, and Functional Properties)
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21 pages, 5088 KiB  
Article
Formation and Characterization of Mycelium–Potato Protein Hybrid Materials for Application in Meat Analogs or Substitutes
by Ramdattu Santhapur, Disha Jayakumar and David Julian McClements
Foods 2024, 13(24), 4109; https://doi.org/10.3390/foods13244109 - 19 Dec 2024
Cited by 3 | Viewed by 2052
Abstract
There is increasing interest in the development of meat analogs due to growing concerns about the environmental, ethical, and health impacts of livestock production and consumption. Among non-meat protein sources, mycoproteins derived from fungal fermentation are emerging as promising meat alternatives because of [...] Read more.
There is increasing interest in the development of meat analogs due to growing concerns about the environmental, ethical, and health impacts of livestock production and consumption. Among non-meat protein sources, mycoproteins derived from fungal fermentation are emerging as promising meat alternatives because of their natural fibrous structure, high nutritional content, and low environmental impact. However, their poor gelling properties limit their application in creating meat analogs. This study investigated the potential of creating meat analogs by combining mycoprotein (MCP), a mycelium-based protein, with potato protein (PP), a plant-based protein, to create hybrid products with meat-like structures and textures. The PP-MCP composites were evaluated for their physicochemical, rheological, textural, and microstructural properties using electrophoresis, differential scanning calorimetry, dynamic shear rheology, texture profile analysis, confocal fluorescence microscopy, and scanning electron microscopy analyses. The PP-MCP hybrid gels were stronger and had more fibrous structures than simple PP gels, which was mainly attributed to the presence of hyphae fibers in mycelia. Dynamic shear rheology showed that the PP-MCP hybrids formed irreversible heat-set gels with a setting temperature of around 70 °C during heating, which was attributed to the unfolding and aggregation of the potato proteins. Confocal and electron microscopy analyses showed that the hybrid gels contained a network of mycelia fibers embedded within a potato protein matrix. The hardness of the PP-MCP composites could be increased by raising the potato protein content. These findings suggest that PP-MCP composites may be useful for the development of meat analogs with more meat-like structures and textures. Full article
(This article belongs to the Special Issue Sustainable Protein Sources: Extraction, Structural Characterization, and Functional Properties)
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