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Egg Protein: Structure and Function

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

Deadline for manuscript submissions: closed (31 December 2022) | Viewed by 44913

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Special Issue Editors

Dr. Long Sheng

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Guest Editor

National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China
Interests: foaming properties; interface characteristic; gel properties; protein interaction; proteomics; protein modification

Prof. Dr. Xiang Duan

E-Mail Website
Guest Editor

College of Food Science and Engineering, Northwest A&F University, Xianyang 712100, China
Interests: egg protein; processing properties; nutrtion and function of proteins

Special Issue Information

Dear Colleagues,

Considering the importance of eggs in the daily diet, the study of their proteins and derived peptides cannot be ignored in food science. How to purify and detect egg protein is the basis for their application. The structure of egg protein needs to be analysed under different processing conditions, and the mechanism of improving processing properties (such as foaming, emulsifying, and gelation) has been a hot topic in this field. Meanwhile, the application of egg protein and derived peptides for the delivery of relevant active substances is of increasing interest due to their broad range of physiological activities. As an essential raw material in food processing, the study of the molecular interactions (protein–polysaccharide and protein–protein) involved in egg protein is also necessary to understand their processing or physiological properties. The potential of egg protein and derived peptides for food production and regulation of human health will continue to attract the attention of researchers.

Dr. Long Sheng
Prof. Dr. Xiang Duan
Guest Editors

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Keywords

egg
protein
peptides
structure
functional properties
interaction
delivery
purification
allergenic
detection

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Published Papers (10 papers)

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Research

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18 pages, 4875 KiB

Open AccessArticle

Egg White and Yolk Protein Atlas: New Protein Insights of a Global Landmark Food

by Eleana Sarantidi, Alexandra Ainatzoglou, Christine Papadimitriou, Eleni Stamoula, Katerina Maghiorou, Argyro Miflidi, Antonia Trichopoulou, Konstantinos C. Mountzouris and Athanasios K. Anagnostopoulos

Foods 2023, 12(18), 3470; https://doi.org/10.3390/foods12183470 - 18 Sep 2023

Cited by 7 | Viewed by 3639

Abstract

(1) Background: The chicken egg is an animal product of great agronomic interest. The egg white and yolk constitute high-quality protein sources for humans with high digestibility and well-balanced amino acid profiles. Despite the egg white and yolk protein’s undisputed value, research to unravel their full proteome content and its properties is still ongoing. We aimed to exhaustively analyze the proteome of egg white and yolk by applying intrinsic proteomics and bioinformatics approaches in order to unravel the full protein potential of this landmark food. (2) Methods: A total of 45 freshly laid, unfertilized, chicken eggs were subjected to nanoLC-MS/MS Orbitrap analysis following a peptide pre-fractionation step. A comprehensive bioinformatics processing step was undertaken towards elucidating potential activities and roles of identified molecules. In parallel, the literature was mined concerning all reported egg white and yolk protein identifications. (3) Results: Our analysis revealed 371 and 428 new proteins, reported for the first time to be present in the egg white and yolk, respectively. From the bioactivity standpoint, egg white and yolk proteins showed high enrichment for antioxidant and anti-inflammatory processes, while exerting high relevance for the apoptosis and focal adhesion pathways. (4) Conclusions: Egg white and yolk proteins exert diverse and multifaceted properties. A total of 799 proteins were reported for the first time as being part of the egg and yolk. Our novel protein data enriched those already published in the literature and the first ever chicken egg white and yolk Protein Atlas, comprising 1392 protein entries, was generated. This dataset will provide a cornerstone reference for future studies involving egg proteins. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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19 pages, 12032 KiB

Open AccessArticle

Characterization of the Dynamic Gastrointestinal Digests of the Preserved Eggs and Their Effect and Mechanism on HepG2 Cells

by Yan Wu, Xiujuan Li, Meihu Ma, Gan Hu, Xing Fu and Jihong Liu

Foods 2023, 12(4), 800; https://doi.org/10.3390/foods12040800 - 13 Feb 2023

Cited by 2 | Viewed by 1940

Abstract

Preserved eggs, an alkaline-fermented food, have been widely searched for their anti-inflammatory activity. Their digestive characteristics in the human gastrointestinal tract and anti-cancer mechanism have not been well explained. In this study, we investigated the digestive characteristics and anti-tumor mechanisms of preserved eggs using an in vitro dynamic human gastrointestinal-IV (DHGI-IV) model. During digestion, the sample pH dynamically changed from 7.01 to 8.39. The samples were largely emptied in the stomach with a lag time of 45 min after 2 h. Protein and fat were significantly hydrolyzed with 90% and 87% digestibility, respectively. Moreover, preserved eggs digests (PED) significantly increased the free radical scavenging activity of ABTS, DPPH, FRAP and hydroxyl groups by 15, 14, 10 and 8 times more than the control group, respectively. PED significantly inhibited the growth, cloning and migration of HepG2 cells at concentrations of 250–1000 μg/mL. Meanwhile, it induced apoptosis by up/down-regulating the expression of the pro-apoptotic factor Bak and the anti-apoptotic gene Bcl-2 in the mitochondrial pathway. PED (1000 μg/mL) treatment resulted in 55% higher ROS production than the control, which also led to apoptosis. Furthermore, PED down-regulated the expression of the pro-angiogenic genes HIF-1α and VEGF. These findings provided a reliable scientific reference for the study of the anti-tumor activity of preserved eggs. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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14 pages, 5156 KiB

Open AccessArticle

Effect of Catechin on Yolk Immunoglobulin Structure and Properties: A Polyphenol–Protein Interaction Approach

by Lili Liu, Xiaodan Zhang, Mapinyi Zhang, Mengjun Zhang, Weiwei Cheng and Baocheng Xu

Foods 2023, 12(3), 462; https://doi.org/10.3390/foods12030462 - 19 Jan 2023

Cited by 8 | Viewed by 2030

Abstract

The preparation of the interaction between polyphenols and protein is of great significance for increasing added value and promoting the application of egg yolk immunoglobulin (IgY). This study systematically investigated the effect of catechin on yolk immunoglobulin structural characteristics and functional properties. The binding conditions, force types, molecular conformation, and residual microenvironment of the interaction between catechin and IgY were analyzed by molecular docking technology, UV-vis absorption and fluorescence spectroscopy studies. The results showed that the main binding forces in the complex were hydrogen bonding and van der Waals forces. After the interaction, fluorescence quenching occurred and the maximum emission wavelength was redshifted. The results showed that the microenvironment around IgY increased polarity, increased hydrophilicity and decreased hydrophobicity, and the structure of the peptide chain changed. The bacteriostatic thermal stability of the compound against Escherichia coli and Staphylococcus aureus was lower than that of catechin IgY. The bacteriostatic acid and base stability were higher than that of catechin and IgY. The antioxidant activity was catechin, complex, and IgY, in descending order. The antioxidant activity of catechin and complex was significantly higher than that of IgY. At the same concentration, the apparent viscosity of the three samples was complex, IgY and catechin, in descending order. G’ was greater than G” indicating that elastic properties dominate in G”. The G’ and G” values of the complex were higher than those of the other groups. Rheological results indicated that the complex may have high physical stability. This study provides theoretical support for broadening the application field of IgY and suggest its properties change in the machining process. It also provides new ideas for the development of functional foods from poultry eggs. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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13 pages, 4305 KiB

Open AccessArticle

Succinylation Modified Ovalbumin: Structural, Interfacial, and Functional Properties

by Gan Hu, Jiemin Zhang, Qi Wang, Meihu Ma, Lulu Ma and Shugang Li

Foods 2022, 11(18), 2724; https://doi.org/10.3390/foods11182724 - 6 Sep 2022

Cited by 17 | Viewed by 2877

Abstract

In this study, ovalbumin (OVA) was succinylated with the addition of different levels of succinic anhydride, and the structural and functional properties of succinylated OVA (SOVA) were investigated. SDS−PAGE and FTIR spectrum confirmed the covalent attachment of the succinyl group to OVA. Thermal stability and the absolute value of zeta potential (pH 6.0) of SOVA were enhanced by 14.90% and 76.77% higher than that of the native OVA (NOVA), respectively. Circular dichroism (CD) spectra demonstrated that the succinylation decreased the α−helix and increased β−sheet content to 21.31% and 43.28%, respectively. The content of free sulfhydryl groups increased and intrinsic fluorescence spectra suggested the SOVA became more unfolded and flexible as the degree of succinylation enhanced. Furthermore, succinylation effectively enhanced the solubility and decreased the interface tension (oil−water and air−water interface) of OVA. Compared to NOVA, the emulsifying activity and stability of SOVA were increased by 1.6 times and 1.2 times, respectively, and foaming capacity and stability were enhanced by 2.7 times and 1.5 times, respectively. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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21 pages, 5462 KiB

Open AccessArticle

The Effects of Phosphorylation and Microwave Treatment on the Functional Characteristics of Freeze-Dried Egg White Powder

by Zahra Jafari, Mohammad Goli and Majid Toghyani

Foods 2022, 11(17), 2711; https://doi.org/10.3390/foods11172711 - 5 Sep 2022

Cited by 11 | Viewed by 2426

Abstract

The effects of phosphorylation pre-treatments at 1.5, 2.5, and 3.5% levels, as well as microwave application at 200, 400, and 700 watts levels for 2 min, on the functional parameters of egg white powder obtained by the freeze dryer procedure were investigated. P1.5-M200 had the highest oil-holding capacity, emulsion stability, and emulsion activity, while P2.5-M200 had the highest foam capacity. The P2.5-M400 had the largest particle size, and P3.5-M200 had the highest degree of phosphorylation and protein solubility. On the other hand, P3.5-M200 had the highest solution viscosity by 1% (w/v), water-holding capacity, and foam stability, in the treatments that used phosphorylation and microwave treatment simultaneously. FTIR spectroscopy of the unfolding structure of egg white protein revealed changes in the protein’s secondary structure, such as the development of β-sheets and β-turns, as well as the binding of negatively charged phosphate groups on the serine, threonine, and tyrosine side chains. The phosphorylation and microwave treatments reduced the particle size of the egg white protein powder while increasing the surface area of the protein molecules, according to SEM analyses. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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17 pages, 3509 KiB

Open AccessArticle

Effects of Peroxyl Radicals on the Structural Characteristics and Fatty Acid Composition of High-Density Lipoprotein from Duck Egg Yolk

by Jing Sun, Qi Zeng, Xue Yang, Jinsong Pi, Meihu Ma and Jinping Du

Foods 2022, 11(11), 1634; https://doi.org/10.3390/foods11111634 - 1 Jun 2022

Cited by 3 | Viewed by 2098

Abstract

In this study, high-density lipoprotein (HDL) from duck egg yolk was subjected to oxidation with a system based on 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH)-derived peroxyl radicals. The effects of peroxyl radicals on the protein carbonyl, free sulfhydryl, secondary/tertiary structure, surface hydrophobicity, solubility, particle size distribution, zeta potential and fatty acid composition of HDL were investigated by using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Fourier-transform infrared spectroscopy (FTIR), circular dichroism (CD), fluorescence spectroscopy, dynamic light scattering and ultra-high-performance liquid chromatography coupled to tandem mass spectrometry (UHPLC-MS/MS). The results indicated that the content of protein carbonyl was significantly increased, that of free sulfhydryl was obviously reduced, and the ordered secondary structure was also decreased with increasing AAPH concentration. In addition, the surface hydrophobicity and solubility of HDL showed apparent increases due to the exposure of hydrophobic groups and aggregation of protein caused by oxidation. The fatty acid composition of HDL exhibited pronounced changes due to the disrupted protein–lipid interaction and lipid oxidation by AAPH-derived peroxyl radicals. These results may help to elucidate the molecular mechanism for the effect of lipid oxidation products on the oxidation of duck yolk proteins. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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17 pages, 3176 KiB

Open AccessArticle

Label-Free LC-MS/MS Analysis Reveals Different Proteomic Profiles between Egg Yolks of Silky Fowl and Ordinary Chickens

by Rao Wu, Chen Chen and Xiaoying Zhang

Foods 2022, 11(7), 1035; https://doi.org/10.3390/foods11071035 - 2 Apr 2022

Cited by 5 | Viewed by 2880

Abstract

The proteomic profiles of Silky fowl egg yolk (SFEY) and Leghorn egg yolk (LEY) were analyzed by bottom-up label-free liquid chromatography–tandem mass spectrometry (LC-MS/MS). From a total of 186 identified proteins, 26 proteins were found significantly differentially abundant between two yolks, of which, 19 were up-regulated and 7 were down-regulated in SFEY, particularly, vitelline membrane outer layer protein 1, transthyretin and ovoinhibitor were up-regulated by 26, 25, and 16 times, respectively. In addition, there were 57 and 6 unique proteins in SFEY and LEY, respectively. Gene Ontology (GO) revealed SFEY contained relatively more abundant protease inhibitors and coagulation-related proteins. Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis revealed differentially abundant proteins in SFEY may be actively involved in the regulation of the neuroactive ligand–receptor interaction pathway. This study provides a theoretical basis for the understanding of proteomic and biological differences between these two yolks and can guide for further exploration of nutritional and biomedical use of Silky fowl egg. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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16 pages, 7477 KiB

Open AccessArticle

Formation of Natural Egg Yolk Granule Stabilized Pickering High Internal Phase Emulsions by Means of NaCl Ionic Strength and pH Change

by Sijie Mi, Minquan Xia, Xinyue Zhang, Jihong Liu and Zhaoxia Cai

Foods 2022, 11(2), 229; https://doi.org/10.3390/foods11020229 - 15 Jan 2022

Cited by 14 | Viewed by 3195

Abstract

Pickering high internal phase emulsions (HIPEs) are gel-like concentrated emulsions that have the potential to be an alternative to partially hydrogenated oil (PHO). In this study, egg yolk granules (EYGs), natural complexes of protein and lipid isolated from egg yolk, were used as an emulsifier to prepare Pickering HIPEs. Gel-like HIPEs with an oil phase volume fraction of 85% and with an emulsifier concentration of only 0.5% could be prepared by using EYGs as an emulsifier. The EYGs were able to form stable HIPEs at NaCl ionic strengths over 0.2 M and at pH over 5.0 with NaCl ionic strength of 0.3 M. The EYGs, which could stabilize HIPEs, were easily to adsorb and cover the oil-water interface to form emulsion droplets with small particle size. In addition, interacting EYGs in the aqueous phase formed a continuous network structure, and the oil droplets packed closely, exhibiting high elasticity and shear thinning behavior. Furthermore, the formed HIPEs had suitable storage stability with no significant changes in appearance and microstructure after storage for 60 days. This work can transform traditional oils from liquid-like to solid-like by using EYGs to enrich food processing diversity and improve the storage stability of oils while reducing the intake of PHO and providing a healthier diet for consumers. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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Review

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19 pages, 1040 KiB

Open AccessReview

Functional Properties and Extraction Techniques of Chicken Egg White Proteins

by Zhe Li, Xi Huang, Qinyue Tang, Meihu Ma, Yongguo Jin and Long Sheng

Foods 2022, 11(16), 2434; https://doi.org/10.3390/foods11162434 - 12 Aug 2022

Cited by 26 | Viewed by 10298

Abstract

Chicken egg whites contain hundreds of proteins, and are widely used in the food, biological and pharmaceutical industries. It is highly significant to study the separation and purification of egg white proteins. This review first describes the structures and functional properties of several major active proteins in egg whites, including ovalbumin, ovotransferrin, ovomucoid, lysozyme, ovomucin, ovomacroglobulin and avidin. Then, the common techniques (including precipitation, chromatography and membrane separation) and some novel approaches (including electrophoresis, membrane chromatography, aqueous two-phase system and molecular imprinting technology) for the separation and purification of egg white proteins broadly reported in the current research are introduced. In addition, several co-purification methods for simultaneous separation of multiple proteins from egg whites have been developed to improve raw material utilization and reduce costs. In this paper, the reported techniques in the last decade for the separation and purification of chicken egg white proteins are reviewed, discussed and prospected, aiming to provide a reference for further research on egg proteins in the future. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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17 pages, 1640 KiB

Open AccessReview

Health Functions of Egg Protein

by Ryosuke Matsuoka and Michihiro Sugano

Foods 2022, 11(15), 2309; https://doi.org/10.3390/foods11152309 - 2 Aug 2022

Cited by 11 | Viewed by 11590

Abstract

Egg protein is a remarkably abundant source of protein, with an amino acid score of 100 and the highest net protein utilization rate. However, there have been relatively fewer studies investigating the health benefits of egg protein. In this review, we have summarized the available information regarding the health benefits of egg proteins based on human studies. In particular, studies conducted on the characteristics of egg whites, as they are high in pure protein, have reported their various health functions, such as increases in muscle mass and strength enhancement, lowering of cholesterol, and visceral fat reduction. Moreover, to facilitate and encourage the use of egg white protein in future, we also discuss its health functions. These benefits were determined by developing an egg white hydrolysate and lactic-fermented egg whites, with the latter treatment simultaneously improving the egg flavor. The health benefits of the protein hydrolysates from the egg yolk (bone growth effect) and eggshell membrane (knee join pain-lowering effect) have been limited in animal studies. Therefore, the consumption of egg protein may contribute to the prevention of physical frailty and metabolic syndromes. Full article

(This article belongs to the Special Issue Egg Protein: Structure and Function)

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