Submit to Molecules Review for Molecules Propose a Special Issue

Journal Menu

Journal Browser

► Journal Browser

Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System

Print Special Issue Flyer
Special Issue Editors
Special Issue Information
Keywords
Published Papers

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

Deadline for manuscript submissions: closed (31 August 2023) | Viewed by 18905

Share This Special Issue

Special Issue Editors

Prof. Dr. Lingyun Chen

E-Mail Website
Guest Editor

Department of Agricultural, Food & Nutritional Science, University of Alberta, Edmonton, AB T6G 2P5, Canada
Interests: proteins; polysaccharides; chemical modifications; structure–function relationships; biopolymeric networks including nano/micro particles; nano-fibers; hydrogels; films
Special Issues, Collections and Topics in MDPI journals

Dr. Liya Liu

E-Mail Website
Guest Editor

Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, China
Interests: pea protein; functional food; food fermentation; interface properties; protein-–polysaccharide interactions
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Food proteins from plant sources such as legumes, cereals, oil seeds and other special crops are increasingly being exploited as more sustainable protein ingredients to address environmental issues and human health concerns. Protein extraction and modification methods are critical to their technico-functional properties, including solubility, rheology, interfacial activity, water and oil binding, emulsifying, foaming and gelling capacity. Depending on the extraction and modification methods, the physicochemical and functional properties of the plant proteins vary significantly, which eventually affects their final application characteristics. Meanwhile, protein fragmentation strategies have also been developed to prepare peptides from plant protein sources with antioxidant, anti-inflammatory, ACE and DPP4 inhibitory activities, among others. This Special Issue aims to capture the latest advances in the extraction and structural modification of plant proteins for new or improved functionality and bioactivity for food, beverage and nutraceutical applications. We welcome articles, communications, and scientific reviews. Relevant topics include but are not limited to the following:

Novel methods and technologies for plant protein extraction and structural modification;
Functionality and bioactivity of plant proteins or hydrolysates in relationship with their structures;
Effective strategies for the applications of functional plant protein ingredients in plant-based food formulations (e.g., meat, beverages, yogurt, whipped cream, ice cream, mayonnaise, staple foods, 3D-printed foods), as well as plant-protein-based delivery systems.

Prof. Dr. Lingyun Chen
Dr. Liya Liu
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. Molecules 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 2700 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

plant protein
extraction
structure modification
functional properties
bioactivities
plant-based food

Published Papers (10 papers)

Download All Papers

Order results

Result details

Show export options Show export options

Select all

Export citation of selected articles as:

Research

Jump to: Review

17 pages, 2708 KiB

Open AccessArticle

Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction

by Andriati Ningrum, Dian Wahyu Wardani, Nurul Vanidia, Manikharda, Achmat Sarifudin, Rima Kumalasari, Riyanti Ekafitri, Dita Kristanti, Woro Setiaboma and Heli Siti Helimatul Munawaroh

Molecules 2023, 28(13), 4974; https://doi.org/10.3390/molecules28134974 - 24 Jun 2023

Cited by 1 | Viewed by 1458

Abstract

Okara is a solid byproduct created during the processing of soy milk. The production of protein hydrolysates utilizing enzymatic tests such as papain can result in the production of bioactive peptides (BPs), which are amino acid sequences that can also be produced from the okara protein by hydrolysis. The objective of this study was to investigate the antioxidant activities of okara hydrolysates using papain, based on the in silico and in vitro assays using the papain enzyme. We found that using the in silico assessment, the antioxidant peptides can be found from the precursor (glycinin and conglycinin) in okara. When used as a protease, papain provides the maximum degree of hydrolysis for antioxidative peptides. The highest-peptide-rank peptide sequence was predicted using peptide ranks such as proline–histidine–phenylalanine (PHF), alanine–aspartic acid–phenylalanine (ADF), tyrosine–tyrosine–leucine (YYL), proline–histidine–histidine (PHH), isoleucine–arginine (IR), and serine–valine–leucine (SVL). Molecular docking studies revealed that all peptides generated from the parent protein impeded substrate access to the active site of xanthine oxidase (XO). They have antioxidative properties and are employed in the in silico approach to the XO enzyme. We also use papain to evaluate the antioxidant activity by using in vitro tests for protein hydrolysate following proteolysis. The antioxidant properties of okara protein hydrolysates have been shown in vitro, utilizing DPPH and FRAP experiments. This study suggests that okara hydrolysates generated by papain can be employed as natural antioxidants in food and for further applications, such as active ingredients for antioxidants in packaging. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

14 pages, 2951 KiB

Open AccessArticle

Effect of Chemical Refining on the Reduction of β-Carboline Content in Sesame Seed Oil

by Lili Shi, Ziyu Cui and Wei Liu

Molecules 2023, 28(11), 4503; https://doi.org/10.3390/molecules28114503 - 01 Jun 2023

Cited by 1 | Viewed by 1210

Abstract

β-carbolines (harman and norharman) are potentially mutagenic and have been reported in some vegetable oils. Sesame seed oil is obtained from roasted sesame seeds. During sesame oil processing, roasting is the key procedure to aroma enhancement, in which β-carbolines are produced. Pressed sesame seed oils cover most market share, while leaching solvents are used to extract oils from the pressed sesame cake to improve the utilization of the raw materials. β-carbolines are nonpolar heterocyclic aromatic amines with good solubility in leaching solvents (n-hexane); therefore, the β-carbolines in sesame cake migrated to the leaching sesame seed oil. The refining procedures are indispensable for leaching sesame seed oil, in which some small molecules can be reduced. Thus, the critical aim is to evaluate the changes in β-carboline content during the refining of leaching sesame seed oil and the key process steps for the removal of β-carbolines. In this work, the levels of β-carbolines (harman and norharman) in sesame seed oil during chemical refining processes (degumming, deacidification, bleaching and deodorization) have been determined using solid phase extraction and high performance liquid chromatography-mass spectrometry (LC-MS). The results indicated that in the entire refining process, the levels of total β-carbolines greatly decreased, and the adsorption decolorization was the most effective process in reducing β-carbolines, which might be related to the adsorbent used in the decolorization process. In addition, the effects of adsorbent type, adsorbent dosage and blended adsorbent on β-carbolines in sesame seed oil during the decolorization process were investigated. It was concluded that oil refining can not only improve the quality of sesame seed oil, but also reduce most of the harmful β-carbolines. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

13 pages, 6586 KiB

Open AccessArticle

Effects of Oat β-Glucan on the Textural and Sensory Properties of Low-Fat Set Type Pea Protein Yogurt

by Peiyao Zhao, Nana Li, Lingyun Chen, Yahong Guo, Yatao Huang, Litao Tong, Lili Wang, Bei Fan, Fengzhong Wang and Liya Liu

Molecules 2023, 28(7), 3067; https://doi.org/10.3390/molecules28073067 - 29 Mar 2023

Cited by 5 | Viewed by 1677

Abstract

This study investigated the effect of oat β-glucan as a fat substitute on the structure formation, texture, and sensory properties of pea protein yogurt. The results showed that the incorporation of 0.5% β-glucan significantly accelerated the lactic acid bacteria-induced fermentation, with the time for reaching the target pH of 4.6 shortened from 3.5 h to 3 h (p < 0.05); increased the plastic module (G′) from 693 Pa to 764 Pa when fermenting 3 h (p < 0.05); and enhanced the water-holding capacity from 77.29% to 82.15% (p < 0.05). The identification of volatile organic compounds (VOCs) in low-fat pea protein yogurt by GC-IMS revealed a significant decrease in aldehydes and a significant increase in alcohols, ketones and acids in the pea yogurt after fermentation (p < 0.05). Among them, the levels of acetic acid, acetone, 2,3-butanedione, 3-hydroxy-2-butanone, and ethyl acetate all significantly increased with the addition of oat β-glucan (p < 0.05), thereby providing prominent fruity, sweet, and creamy flavors, respectively. Combined with the results of sensory analysis, the quality characteristics of pea protein yogurt with 1% oil by adding 1% oat β-glucan were comparable to the control sample with 3% oil. Therefore, oat β-glucan has a good potential for fat replacement in pea protein yogurt. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

16 pages, 3936 KiB

Open AccessArticle

Effect of Protein-Glutaminase on Calcium Sulphate-Induced Gels of SPI with Different Thermal Treatments

by Xin Li, Liwei Fu, Zhiyong He, Maomao Zeng, Qiuming Chen, Fang Qin, Zhaojun Wang and Jie Chen

Molecules 2023, 28(4), 1752; https://doi.org/10.3390/molecules28041752 - 12 Feb 2023

Cited by 2 | Viewed by 1365

Abstract

The effects of protein-glutaminase (PG) on calcium sulphate (CaSO₄)-induced gels of soy protein isolate (SPI) with different heat treatment levels were investigated. The time-dependent degree of deamidation showed that the mild denaturation of the protein favored the deamidation. The particle size distribution showed that the heat treatment increased the SPI particle size, and the particle size distribution of the SPI shifted to the right or increased the proportion of the large particle size component as the degree of deamidation increased for each sample. Rheological analysis showed that the deamidation substantially pushed up the gel temperature and decreased the value of G′. The gel strength and water-holding capacity showed that the higher the amount of enzyme added, the more significant the decrease in gel strength, while the gel water-holding capacity increased. In summary, the deamidation of PG and heat treatment can affect the gel properties of SPI synergistically. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

11 pages, 2226 KiB

Open AccessArticle

Effect of Thermal Treatment on the Self-Assembly of Wheat Gluten Polypeptide

by Hao Liu, Jingxuan Wang, Mei Liu, Xia Zhang, Ying Liang and Jinshui Wang

Molecules 2023, 28(2), 834; https://doi.org/10.3390/molecules28020834 - 14 Jan 2023

Cited by 2 | Viewed by 1401

Abstract

Self-assembled fibrillation of wheat gluten is a common phenomenon in the daily production and processing of wheat flour products. The driving forces for its formation and the factors that influence the morphology of fibrils have not been thoroughly investigated. In this study, the effect of three bonding changes (breaking hydrogen bonds, strengthening hydrophobic interactions, and SH-SS exchange reactions) on gluten polypeptide (GP) fibrillation was simulated by adjusting the heating temperature (room temperature (RT), 45 °C, 65 °C, and 95 °C). The results showed that the breakage of hydrogen bonds could induce conformational transitions in GPs and help to excite fibrillation in GPs. Strengthened hydrophobic interactions significantly contributed to the fibrillation of GPs. Covalent crosslinks generated by SH-SS exchange reactions might also promote the fibrillation of GPs. GPs with different degrees of hydrolysis (4.0%, 6.0%, and 10.0%, represented by DH 4, DH 6, and DH 10, respectively) presented different extents of fibrillation, with DH 10 GPs having a higher propensity to fibrillation than DH 4 and DH 6 GPs. The results of Fourier’s transform infrared spectroscopy indicated that hydrophobic interactions drive the transition from a random coil and α-helix to a β-sheet. In addition, hydrophobic interactions also drive the intermolecular polymerization of GPs, resulting in larger molecular weight aggregates. The morphology presented by transmission electron microscopy showed that the greater the DH, the stronger the tendency for the worm-like aggregation of GPs. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

21 pages, 2598 KiB

Open AccessArticle

Influence of the Enzymatic Hydrolysis Using Flavourzyme Enzyme on Functional, Secondary Structure, and Antioxidant Characteristics of Protein Hydrolysates Produced from Bighead Carp (Hypophthalmichthys nobilis)

by Kamal Alahmad, Anwar Noman, Wenshui Xia, Qixing Jiang and Yanshun Xu

Molecules 2023, 28(2), 519; https://doi.org/10.3390/molecules28020519 - 05 Jan 2023

Cited by 7 | Viewed by 2910

Abstract

In the current study, bighead carp fish were used in conjunction with the flavourzyme enzyme to obtain (FPH) fish protein hydrolysates. The optimum conditions of the hydrolysis process included an enzyme/substrate ratio of 4% and a temperature of 50 °C and pH of 6.5. The hydrolysis time was studied and investigated at 1, 3, and 6 h, and the (DH) degree of hydrolysis was recorded at 16.56%, 22.23%, and 25.48%, respectively. The greatest yield value was 17.83% at DH 25.48%. By increasing the DH up to 25.48%, the crude protein and total amino acid composition of the hydrolysate were 88.19% and 86.03%, respectively. Moreover, more peptides with low molecular weight were formed during hydrolysis, which could enhance the functional properties of FPH, particularly the solubility property ranging from 85% to 97%. FTIR analysis revealed that enzymatic hydrolysis impacted the protein’s secondary structure, as indicated by a remarkable wavelength of amide bands. Additionally, antioxidant activities were investigated and showed high activity of DDPH radical scavenging, and hydroxyl radical scavenging demonstrated remarkable activity. The current findings demonstrate that the functional, structural, and antioxidant characteristics of FPH might make it an excellent source of protein and suggest potential applications in the food industry. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

15 pages, 1895 KiB

Open AccessArticle

Screening and Mechanism of Novel Angiotensin-I-Converting Enzyme Inhibitory Peptides in X. sorbifolia Seed Meal: A Computer-Assisted Experimental Study Method

by Yihan Mu, Dongwei Liu, Huaping Xie, Xinyu Zhang, Xue Han and Zhaolin Lv

Molecules 2022, 27(24), 8792; https://doi.org/10.3390/molecules27248792 - 12 Dec 2022

Cited by 1 | Viewed by 1265

Abstract

Angiotensin-I-converting enzyme (ACE) inhibitors are used extensively to control hypertension. In this study, a computer-assisted experimental approach was used to screen ACE-inhibiting peptides from X. sorbifolum seed meal (XSM). The process conditions for XSM hydrolysis were optimized through the orthogonal experimental method combined with a database. The optimal conditions for ACE inhibition included an alkaline protease dose of 5%, 45 °C, 15 min and pH 9.5. The hydrolysate was analyzed by LC-MS/MS, and 10 optimal peptides were screened. Molecular docking results revealed four peptides (GGLPGFDPA, IMAVLAIVL, ETYFIVR, and INPILLPK) with ACE inhibitory potential. At 0.1 mg/mL, the synthetic peptides GGLPGFDPA, ETYFIVR, and INPILLPK provided ACE inhibition rates of 24.89%, 67.02%, and 4.19%, respectively. GGLPGFDPA and ETYFIVR maintained high inhibitory activities during in vitro digestions. Therefore, the XSM protein may be a suitable material for preparing ACE inhibitory peptides, and computer-assisted experimental screening is an effective, accurate and promising method for discovering new active peptides. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

16 pages, 3769 KiB

Open AccessArticle

The Consistency Factor and the Viscosity Exponent of Soybean-Protein-Isolate/Wheat-Gluten/Corn-Starch Blends by Using a Capillary Rheometry

by Wei Zhang, Donglin Zhao, Ziyan Dong, Jian Li, Bo Zhang and Wenhua Yu

Molecules 2022, 27(19), 6693; https://doi.org/10.3390/molecules27196693 - 08 Oct 2022

Cited by 1 | Viewed by 1340

Abstract

Blends with different proportions of protein or starch show different rheological behaviors, which may be related to the fibrous structure formation of extruded textured plant proteins. The consistency factor K and the viscosity exponent n of soybean–protein–isolate (SPI)/wheat–gluten (WG)/corn–starch (CS) blends were investigated through capillary rheometry. All blends exhibited shear-thinning behavior at 80 °C and 50% moisture. The CS content in SPI/CS blends or WG content in SPI/WG blends showed a positive relation to the viscosity exponent n and a negative relation to the consistency factor K. However, there was no correlation between the CS content in WG/CS blends and n or K. The coefficient of determination of the linear relationship between K and mass fraction in SPI/CS, SPI/WG/CS, SPI/WG and WG/CS decreased from 0.872 to 0.073. SPI was more likely to form a non-interactive structure, while wheat-gluten was more likely to form a highly interactive structure. It turned out that the materials with globular morphology, such as soybean-protein-isolate and corn-starch, are likely to form a non-interactive structure. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

14 pages, 1404 KiB

Open AccessArticle

Influence of the Degree of Hydrolysis on Functional Properties and Antioxidant Activity of Enzymatic Soybean Protein Hydrolysates

by Monirul Islam, Yatao Huang, Serajul Islam, Bei Fan, Litao Tong and Fengzhong Wang

Molecules 2022, 27(18), 6110; https://doi.org/10.3390/molecules27186110 - 19 Sep 2022

Cited by 20 | Viewed by 3306

Abstract

Soybean protein hydrolysates were prepared using two proteolytic enzymes (Alcalase and Protamex) and the degree of hydrolysis (DH) and their functional and antioxidant properties were evaluated. The highest DH value was 20%, with a yield of 19.77% and protein content of 51.64%. The total amino acid content was more than 41% for all protein hydrolysates. The protein hydrolysates from Protamex at pH 2.0 had excellent solubility, emulsifying activity, and foaming capacity, at 83.83%, 95.03 m²/g, and 93.84%, respectively. The water-holding capacity was 4.52 g/g for Alcalase, and the oil-holding capacity was 4.91 g/g for Protamex. The antioxidant activity (62.07%), as measured by the samples’ reaction with DPPH (2,2-diphenyl-1-picrylhydrazyl) and the reducing power (0.27) were the strongest for Protamex. An ABTS activity rate of 70.21% was recorded for Alcalase. These findings indicated a strong potential for the utilization of soybean protein hydrolysates to improve the functional properties and antioxidant activity of soybeans as well as their nutritional values. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Figure 1

Review

Jump to: Research

20 pages, 1806 KiB

Open AccessReview

A Review of Plant Selenium-Enriched Proteins/Peptides: Extraction, Detection, Bioavailability, and Effects of Processing

by Yangyang Xiong, Yatao Huang, Lin Li, Yanfang Liu, Liya Liu, Lili Wang, Litao Tong, Fengzhong Wang and Bei Fan

Molecules 2023, 28(3), 1223; https://doi.org/10.3390/molecules28031223 - 26 Jan 2023

Cited by 7 | Viewed by 1921

Abstract

As an essential trace element in the human body, selenium (Se) has various physiological activities, such as antioxidant and anticancer activity. Selenium-enriched proteins/peptides (SePs/SePPs) are the primary forms of Se in plants and animals, and they are the vital carriers of its physiological activities. On the basis of current research, this review systematically describes the extraction methods (aqueous, alkaline, enzymatic, auxiliary, etc.) and detection methods (HPLC–MS/MS, GC–ICP-MS, etc.) for SePs/SePPs in plants. Their bioavailability and bioactivity, and the effect of processing are also included. Our review provides a comprehensive understanding and theoretical guidance for the utilization of selenium-enriched proteins/peptides. Full article

(This article belongs to the Special Issue Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System)

► Show Figures

Journal Menu

Journal Browser

Extraction, Modification, Functionality and Bioactivity of Plant Proteins for a Healthy and Sustainable Food System

Share This Special Issue

Special Issue Editors

Special Issue Information

Keywords

Published Papers (10 papers)

Research

Review

Further Information

Guidelines

MDPI Initiatives

Follow MDPI