Quantitative proteomic analysis of chicken egg white and its components
[Display omitted] •A total of 173 proteins were identified in the EW and its there components.•Ovomucin and lysozyme are the main differential proteins of TKEW and TNEW.•Mutual validation of various properties of egg whites with the proteome.•The most of the 61 unique proteins in the CLZ originate f...
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Published in | Food research international Vol. 170; p. 113019 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Canada
Elsevier Ltd
01.08.2023
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Subjects | |
Online Access | Get full text |
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Summary: | [Display omitted]
•A total of 173 proteins were identified in the EW and its there components.•Ovomucin and lysozyme are the main differential proteins of TKEW and TNEW.•Mutual validation of various properties of egg whites with the proteome.•The most of the 61 unique proteins in the CLZ originate from the egg yolk.•A total of 28 DAPS were identified by screening between EW and CLZ.
The protein profiles and properties of chicken egg white and its three components (thick egg white, TKEW; thin egg white, TNEW; and chalaza, CLZ) were comprehensively compared. The proteomes of TNEW and TKEW are relatively similar, but the abundance of mucin-5B and mucin-6 (the two subunits of ovomucin) is significantly higher in TKEW than in TNEW (42.97% and 870.04%, respectively), while the lysozymes in TKEW are 32.57% higher (p < 0.05) than those in TNEW. Meanwhile, the properties (including the spectroscopy, viscosity, and turbidity) of TKEW and TNEW are significantly different. Comprehensively, it is speculated that the electrostatic interactions between lysozyme and ovomucin are the main reason for the high viscosity and turbidity of TKEW. Compared with egg white sample (EW), CLZ has a higher abundance of insoluble proteins (mucin-5B, 4.23-fold; mucin-6, 6.89-fold) and a lower abundance of soluble proteins (ovalbumin-related protein X, 89.35% lower than EW; ovalbumin-related protein Y, 78.51% lower; ovoinhibitor, 62.08% lower; riboflavin-binding protein, 93.67% lower). These compositional differences should explain the insolubility of CLZ. These findings are important references for deepening the research and development of egg white in the future, such as the thinning of egg white, the molecular basis of changes in egg white properties, and the differential application of TKEW and TNEW. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0963-9969 1873-7145 |
DOI: | 10.1016/j.foodres.2023.113019 |