Chicken egg white —  characteristics of its properties and the prospects for functional foods development

The overview presents the literature data and the results of our own research on prospects of using the chicken eggs as the basis of functional foods. The composition of chicken eggs and their components, characteristics of egg white proteins properties are presented thereto. The biologically active compounds included into egg composition are analyzed. The data on the biological value of egg white are given. The characteristic of egg white foaming ability is presented. It has been shown that the ability of proteins to form stable intermolecular structures, especially with partially denaturated proteins, allows them forming viscoelastic superficial films that ensure foam stability. The high foaming ability of chicken egg protein macromolecules is directly related to their interphase properties, i. e. the ability to form interphase layers at the “liquid — gas” interface. The foaming properties of the various egg proteins are not equal, and therefore they contribute to foaming properties at various extents. The model of egg white proteins gelation is considered and the factors influencing the gelation process are described. It has been shown that very important changes in proteins properties are caused by denaturation. The proteins lose their ability to hydrate; the protective aqueous shell around the globules disappears, the proteins stick together, grow larger and lose solubility. This process is called coagulation. The influence of denaturation and aggregation on variations of protein properties is described below. Data on protein fortification with functional ingredients (calcium, iodine, plant polyphenols) and creation of functional egg and meat foods are presented here.

Download Full-text

DEVELOPMENT AND IN VIVO EVALUATION OF COMPLEXES OF BIOLOGICALLY ACTIVE COMPOUNDS WITH BIOPOLYMER MATRICES

10.47501/978-5-6044060-1-4.36 ◽

2021 ◽

Author(s):

Nikita Aleksandrovich Petrov ◽

◽

Yuliya Sergeevna Sidorova ◽

Alla Alekseevna Kochetkova ◽

Vladimir Kimovich Mazo ◽

...

Keyword(s):

Egg White ◽

Biologically Active Compounds ◽

Biologically Active ◽

In Vivo Evaluation ◽

Active Compounds ◽

Food Ingredients ◽

Chicken Egg ◽

Buckwheat Flour

The paper presents the results of a preclinical assessment of the effectiveness of food ingredients: a concentrate of blueberry leaf polyphenols sorbed on buckwheat flour, and a concentrate of phytoecdysteroid 20-hydroxyecdysone and quinoa grain flavonoids sorbed on chicken egg white.

Download Full-text

Effect of Xanthan and Arabic Gums on Foaming Properties of Pumpkin (Cucurbita pepo) Seed Protein Isolate

Journal of Food Research ◽

10.5539/jfr.v3n1p87 ◽

2013 ◽

Vol 3 (1) ◽

pp. 87 ◽

Cited By ~ 1

Author(s):

Quirino Dawa ◽

Yufei Hua ◽

Moses Vernonxious Madalitso Chamba ◽

Kingsley George Masamba ◽

Caimeng Zhang

Keyword(s):

Sodium Chloride ◽

Salt Concentration ◽

Seed Protein ◽

Foam Stability ◽

Chloride Concentration ◽

Egg White ◽

Protein Isolate ◽

Foaming Properties ◽

Ph Optimum ◽

Pumpkin Seed

Understanding how foaming properties of proteins are affected by factors such as pH, salt concentration and temperature is essential in predicting their performance and utilisation. In this study, the effects of pH and salt concentration were studied on the foaming properties of pumpkin seed protein isolate (PSPI) and PSPI- xanthan (XG)/Arabic (GA) gum blends. The foaming properties of the PSPI-GA/XG blends were also compared with egg white. Foam stability (FS) was significantly affected by pH with PSPI: GA (25:4) and PSPI: XG (25:1) having a significantly higher stability at pH 2 with the lowest foam stability at pH 4. Sodium chloride (0.2-1.0 M) did not significantly affect foaming properties although PSPI: GA (25:4) had the highest FC (89.33 ± 3.24%) and FS (76.83 ± 1.53 min) at 0.2 M sodium chloride concentration. The foaming capacity (FC) of PSPI: GA (25:4) blend (128.00 ± 0.91%) was significantly higher (p < 0.05) than that of egg white (74.00 ± 1.33%) but its FS was significantly lower. It was further revealed that the FC of egg white (74.00 ± 1.33%) was comparable to the PSPI:XG (25:1) blend (74.00 ± 1.46%) but the FS for egg white (480.00 ± 2.67 min) was significantly higher (p < 0.05) than the FS (116.21 ± 0.86 min) of PSPI:XG (25:1). The foaming properties of PSPI and PSPI-xanthan (XG)/Arabic (GA) blends were significantly affected by pH. Optimum foaming properties, PSPI:XG (25:1) and PSPI:GA (25:4) were observed at pH 2 and heat treatment temperature of 80 ºC.

Download Full-text

Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides

Foods ◽

10.3390/foods9091312 ◽

2020 ◽

Vol 9 (9) ◽

pp. 1312

Author(s):

Pei-Gee Yap ◽

Chee-Yuen Gan

Keyword(s):

Bioactive Peptides ◽

Egg White ◽

Degree Of Hydrolysis ◽

Hydrolysis Time ◽

Relationship Analysis ◽

Activity Inhibition ◽

Chicken Egg ◽

Egg White Proteins ◽

Inhibitory Activities ◽

Active Fragments

Active fragments (bioactive peptides) from the chicken egg white proteins were expected to exert tyrosinase inhibitory activities in which skin hyperpigmentation could be prevented. Egg white was hydrolyzed by trypsin, chymotrypsin and the combination of both enzymes. The enzyme treatments achieved >50% degree of hydrolysis (DH) at substrate-to-enzyme (S/E) ratio of 10–30 (w/w) and hydrolysis time of 2–5 h. A crossed D-optimal experimental design was then used to determine the optimal enzyme composition, S/E ratio and hydrolysis time in order to yield hydrolysates with strong monophenolase and diphenolase inhibitory activities. The optimized conditions 55% trypsin, 45% chymotrypsin, S/E 10:1 w/w and 2 h achieved 45.9% monophenolase activity inhibition whereas 100% trypsin, S/E 22.13:1 w/w and 3.18 h achieved 48.1% diphenolase activity inhibition. LC/MS and MS/MS analyses identified the peptide sequences and the subsequent screening had identified 7 peptides (ILELPFASGDLLML, GYSLGNWVCAAK, YFGYTGALRCLV, HIATNAVLFFGR, FMMFESQNKDLLFK, SGALHCLK and YFGYTGALR) as the potential inhibitor peptides. These peptides were able to bind to H85, H94, H259, H263, and H296 (hotspots for active residues) as well as F92, M280 and F292 (stabilizing residues) of tyrosinase based on structure-activity relationship analysis. These findings demonstrated the potential of egg white-derived bioactive peptides as skin health therapy.

Download Full-text

Functional Properties of Protein from Frozen Mantle and Fin of Jumbo Squid Dosidicus gigas in Function of pH and Ionic Strength

Food Science and Technology International ◽

10.1177/1082013210367157 ◽

2010 ◽

Vol 16 (5) ◽

pp. 451-458 ◽

Cited By ~ 9

Author(s):

J.G. Rocha-Estrada ◽

J.H. Córdova-Murueta ◽

F.L. García-Carreno

Keyword(s):

Connective Tissue ◽

Functional Properties ◽

Salt Concentration ◽

Foam Stability ◽

High Strength ◽

Foaming Properties ◽

Dosidicus Gigas ◽

Jumbo Squid ◽

Sds Page ◽

Protein Properties

Functional properties of protein from mantle and fin of the jumbo squid Dosidicus gigas were explained based on microscopic muscle fiber and protein fractions profiles as observed in SDS-PAGE. Fin has higher content of connective tissue and complex fiber arrangement, and we observed higher hardness of fin gels as expected. Myosin heavy chain (MHC) was found in sarcoplasmic, myofibril and soluble-in-alkali fractions of mantle and only in sarcoplasmic and soluble-in-alkali fractions of fin. An additive effect of salt concentration and pH affected the solubility and foaming properties. Fin and mantle proteins yielded similar results in solubility tests, but significant differences occurred for specific pH and concentrations of salt. Foaming capacity was proportional to solubility; foam stability was also affected by pH and salt concentration. Hardness and fracture strength of fin gels were significantly higher than mantle gels; gels from proteins of both tissues reached the highest level in the folding test. Structural and molecular properties, such as MHC and paramyosin solubility, arrangement of muscle fibers and the content of connective tissue were useful to explain the differences observed in these protein properties. High-strength gels can be formed from squid mantle or fin muscle. Fin displayed similar or better properties than mantle in all tests.

Download Full-text

Comparative Study on Foaming Properties of Egg White with Yolk Fractions and Their Hydrolysates

Foods ◽

10.3390/foods10092238 ◽

2021 ◽

Vol 10 (9) ◽

pp. 2238

Author(s):

Xin Li ◽

Yue-Meng Wang ◽

Cheng-Feng Sun ◽

Jian-Hao Lv ◽

Yan-Jun Yang

Keyword(s):

Foam Stability ◽

Egg Yolk ◽

Egg White ◽

Foaming Properties ◽

Foaming Agent ◽

Yolk Granules ◽

Industrial Processing ◽

Egg White Protein ◽

Egg Yolk Plasma ◽

Yolk Plasma

As an excellent foaming agent, egg white protein (EWP) is always contaminated by egg yolk in the industrial processing, therefore, decreasing its foaming properties. The aim of this study was to simulate the industrial EWP (egg white protein with 0.5% w/w of egg yolk) and characterize their foaming and structural properties when hydrolyzed by two types of esterase (lipase and phospholipase A2). Results showed that egg yolk plasma might have been the main fraction, which led to the poor foaming properties of the contaminated egg white protein compared with egg yolk granules. After hydrolyzation, both foamability and foam stability of investigated systems thereof (egg white protein with egg yolk, egg white protein with egg yolk plasma, and egg white protein with egg yolk granules) increased significantly compared with unhydrolyzed ones. However, phospholipids A2 (PLP) seemed to be more effective on increasing their foaming properties as compared to those systems hydrolyzed by lipase (LP). The schematic diagrams of yolk fractions were proposed to explain the aggregation and dispersed behavior exposed in their changes of structures after hydrolysis, suggesting the aggregated effects of LP on yolk plasma and destructive effects of PLP on yolk granules, which may directly influence their foaming properties.

Download Full-text