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Functional Properties of Food Proteins

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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 (30 June 2023) | Viewed by 9675

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Special Issue Editors

Dr. Lina Zhang

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Guest Editor

State Key Laboratory of Food Science & Technology, Jiangnan University, Wuxi 214122, China
Interests: dairy products; proteomics; milk processing; milk allergy, protein structure; protein functionality; diabetes

Prof. Dr. Yulong Bao

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Guest Editor

School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China
Interests: meat and aquatic products; plant proteins; protein physiochemistry; protein functionality; freezing
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Dear Colleagues,

Functional properties (texture formation, gelation, emulsification, water-holding, etc.) have been widely studied with traditional protein sources. Recently, there has been an increasing interest in the production and utilization of novel protein ingredients in foods, including those derived from plants, insects, algae, other microorganisms, etc. The physicochemical properties of these proteins and hence their functional effects in food can be quite different from those of traditional ones. The functional properties of food proteins have been largely studied in test tubes and the like. However, real foods are much more complex; their biochemical reactions can be quite different from those in test tubes. The interaction of proteins with other food components in real food needs to be addressed as well. In addition, studies on food proteins could benefit from the ongoing development of protein science and technical approaches.

Proteomics is a new area of study involving proteome, phosphorylated proteome, and glycosylated proteome profiling using mass spectrometry. It represents a fundamental research tool for protein characterization and biomarker discovery. Recently, proteomics has also been used to study the complexity of the proteome in food science. A wide range of techniques for the identification and quantification of the relatively low abundance of protein in food have been developed, including (but not limited to) high-throughput-screening-based non-targeted methods, such as shotgun proteomics, TMT labeling, iTRAQ labeling, etc.), ion-mobility-based 4D proteomics, and high-precise targeted methods, such as multiple reaction monitoring (MRM), parallel reaction monitoring (PRM), etc. These techniques help us to better understand the biological function of food proteins and the interactions of proteins with other components.

This Special Issue aims to collect basic and applied research focusing on the functional properties of food proteins using either proteomics techniques or other fundamental approaches. Original research and review articles offering insights or solutions regarding improving the functionality of food proteins are welcome.

Dr. Lina Zhang
Prof. Dr. Yulong Bao
Guest Editors

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Keywords

protein chemistry
protein physics
protein modification
proteomic techniques
interaction
food matrix
storage
processing

Published Papers (6 papers)

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Research

15 pages, 3857 KiB

Open AccessArticle

Electron Beam Irradiation Alters the Physicochemical Properties of Chickpea Proteins and the Peptidomic Profile of Its Digest

by Yaqi Zhang, Yunfei Kong, Wanjun Xu, Zhen Yang and Yulong Bao

Molecules 2023, 28(16), 6161; https://doi.org/10.3390/molecules28166161 - 21 Aug 2023

Cited by 3 | Viewed by 1034

Abstract

Irradiation can be used for the preservation of chickpea protein as it can destroy microorganisms, bacteria, virus, or insects that might be present. However, irradiation may provoke oxidative stress, and therefore modify the functionality and nutritional value of chickpea protein. In order to study the effects of irradiation on the physicochemical properties and digestion behaviour of chickpea protein, chickpea protein concentrate (CPC) was treated with electron beam irradiation (EBI) at doses of 5, 10, 15, and 20 kGy. After irradiation, protein solubility first increased at 10 kGy and 15 kGy, and then decreased at the higher dose of 20 kGy. This was supported by SDS-PAGE, where the intensity of major protein bands first increased and then decreased. Increased doses of EBI generally led to greater oxidative modification of proteins in CPC, indicated by reduced sulfhydryls and increased carbonyls. In addition, the protein structure was modified by EBI as shown by Fourier transform infrared spectroscopy analysis, where α-helix generally decreased, and β-sheet increased. Although the protein digestibility was not significantly affected by EBI, the peptidomic analysis of the digests revealed significant differences among CPC irradiated with varying doses. A total of 337 peptides were identified from CPC irradiated with 0 kGy, 10 kGy, and 20 kGy, with 18 overlapping peptides and 60, 29, and 40 peptides specific to the groups of 0, 10, and 20 kGy respectively. Theoretical calculation showed that the distribution of peptide length, hydrophobicity, net charge, and C-terminal residues were affected by irradiation. The 2, 2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity showed a marginal decrease with an increasing dose of irradiation. In conclusion, EBI led to oxidative modification and structural changes in chickpea protein, which subsequently affected the physicochemical properties of peptides obtained from in-vitro digestion of CPC, despite similar digestibility. Full article

(This article belongs to the Special Issue Functional Properties of Food Proteins)

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10 pages, 1187 KiB

Open AccessArticle

The Composition, Structure, and Functionalities of Prolamins from Highland Barley

by Jinjin Xing, Zhaomin Li, Wenhui Zhang and Pengjie Wang

Molecules 2023, 28(14), 5334; https://doi.org/10.3390/molecules28145334 - 11 Jul 2023

Viewed by 1145

Abstract

The composition, structure, and functionalities of prolamins from highland barley were investigated. These parameters were compared with those of the commonly applied prolamins (zein). There are more charged and hydrophilic amino acids in highland barely prolamins than zein. The molecular weight of highland barely prolamins was between 30 and 63 kDa, which was larger than that of zein (20 and 24 kDa). The main secondary structure of highland barely prolamins was β-turn helices, while α-helical structures were the main secondary structure in zein. The water holding capacity, thermal stability, emulsifying capacity, and stability of prolamins from highland barley were significantly higher than in zein, while the opposite results were observed for oil absorption capacity between the two. The diameter of fibers prepared using highland barely prolamins was almost six times that of zein, while highland barely prolamins formed ribbon structures instead of fibers. Therefore, the results provide guidance for applications of prolamins from highland barley. Full article

(This article belongs to the Special Issue Functional Properties of Food Proteins)

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18 pages, 3239 KiB

Open AccessArticle

Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment

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

Molecules 2022, 27(23), 8221; https://doi.org/10.3390/molecules27238221 - 25 Nov 2022

Cited by 6 | Viewed by 1590

Abstract

This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (p < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (p < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition. Full article

(This article belongs to the Special Issue Functional Properties of Food Proteins)

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19 pages, 3734 KiB

Open AccessArticle

Process Optimization, Amino Acid Composition, and Antioxidant Activities of Protein and Polypeptide Extracted from Waste Beer Yeast

by Lisha Zhu, Jianfeng Wang, Yincheng Feng, Hua Yin, Huafa Lai, Ruoshi Xiao, Sijia He, Zhaoxia Yang and Yi He

Molecules 2022, 27(20), 6825; https://doi.org/10.3390/molecules27206825 - 12 Oct 2022

Cited by 5 | Viewed by 1999

Abstract

Repurposing of waste beer yeast (WBY) that a main by-product of brewing industry has attracted considerable attention in recent years. In this study, the protein and polypeptide were extracted by ultrasonic-assisted extraction and enzymatic hydrolysis with process optimization, which resulted in a maximum yield of 73.94% and 61.24%, respectively. Both protein and polypeptide of WBY were composed of 17 Amino acids (AA) that included seven essential amino acids (EAA), and typically rich in glutamic acid (Glu) (6.46% and 6.13%) and glycine (Gly) (5.26% and 6.02%). AA score (AAS) revealed that the threonine (Thr) and SAA (methionine + cysteine) were the limiting AA of WBY protein and polypeptide. Furthermore, the antioxidant activities of WBY polypeptide that lower than 10 kDa against hydroxyl radical, DPPH radical, and ABTS radical were 95.10%, 98.37%, and 69.41%, respectively, which was significantly higher than that of WBY protein (25–50 kDa). Therefore, the protein and polypeptide extracted from WBY can be a source of high-quality AA applying in food and feed industry. Due to small molecular weight, abundant AA, and great antioxidant activity, WBY polypeptide can be promisingly used as functional additives in the pharmaceutical and healthcare industry. Full article

(This article belongs to the Special Issue Functional Properties of Food Proteins)

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11 pages, 957 KiB

Open AccessArticle

Evaluating the Functional Characteristics of Certain Insect Flours (Non-Defatted/Defatted Flour) and Their Protein Preparations

by Ewelina Zielińska

Molecules 2022, 27(19), 6339; https://doi.org/10.3390/molecules27196339 - 26 Sep 2022

Cited by 9 | Viewed by 1884

Abstract

Edible insects as an alternative source of protein are gaining increasing attention, leading to new opportunities for their use in food processing. In this study, the functional properties, such as water and oil holding capacity, foaming, and emulsifying properties, of the most popular insect forms (flour, defatted flour, and protein preparations), such as Gryllus asimillis, Acheta domesticus, and Zophobas morio, were studied. Moreover, proximate analysis, protein extraction yield and efficiency, and sensory analysis, were evaluated. Defatting the flours yielded the highest protein content of all the insect forms tested, in the range of 70.51 to 76.02%, significantly reducing their calorific value by up to 35% for Z. morio. Generally, protein preparations exhibit the best functional properties among studied forms, and the most significant differences are noticeable in foaming capacity—near 30% higher than flours. Furthermore, all samples scored well in the sensory test (overall score 3.76–4.47) except for the Z. morio flour (2.93), which may exclude it from being used in the food industry. The results show that the insect forms studied, due to their good functional properties, can become a valuable component of food recipes, positively impacting the characteristics of the designed food. Full article

(This article belongs to the Special Issue Functional Properties of Food Proteins)

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17 pages, 1062 KiB

Open AccessArticle

Targeted Bottom–Up Mass Spectrometry Approach for the Relative Quantification of Post-Translational Modification of Bovine κ-Casein during Milk Fermentation

by Sorel Tchewonpi Sagu, Harshadrai M. Rawel and Sascha Rohn

Molecules 2022, 27(18), 5834; https://doi.org/10.3390/molecules27185834 - 08 Sep 2022

Cited by 2 | Viewed by 1403

Abstract

κ-casein (κ-CN) is one of the key components in bovine milk, playing a unique role in the structuration of casein micelles. It contains in its chemical structure up to sixteen amino acid residues (mainly serine and threonine) susceptible to modifications, including glycosylation and phosphorylation, which may further be formed during milk processing. In this study, changes in post-translational modification (PTM) of κ-CN during bovine milk fermentation were investigated. One-to-five-day fermented milk samples were produced. A traditional bottom–up proteomics approach was used to establish a multiple-reaction monitoring (MRM) method for relative quantification of κ-CN PTM. Endoproteinase Glu-C was found to efficiently digest the κ-CN molecule. The developed LC-MS method was validated by performing assessments of linearity, precision, repeatability, reproducibility, limit of detection (LOD), and limit of quantification (LOQ). Among the yielded peptides, four of them containing serine and threonine residues were identified and the unmodified as well as the modified variants of each of them were relatively quantified. These peptides were (1) IPTINTIASGEPTSTTE _{[140, 158]}, (2) STVATLE _{[162, 168]}, (3) DSPE _{[169, 172]}, and (4) INTVQVTSTAV _{[180, 190]}. Distribution analysis between unmodified and modified peptides revealed that over 50% of κ-CN was found in one of its modified forms in milk. The fermentation process further significantly altered the composition between unmodified/modified κ-CN, with glycoslaytion being predominant compared to phosphorylation (p < 0.01). Further method development towards α and β-CN fractions and their PTM behavior would be an asset to better understand the changes undergone by milk proteins and the micellar structure during fermentation. Full article

(This article belongs to the Special Issue Functional Properties of Food Proteins)

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