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Updated: Feb 28, 2026
Mechanical Separation and Protein Solubilization of the Outer and Inner Perivitelline Sublayers from Hen's Eggs
Published on: January 27, 2021
Quantitative proteomic analysis reveals the role of tea polyphenol EGCG in egg whites in response to vanadium stress
Jianping Wang1, Xue Bai1, Xuemei Ding1
1Animal Nutrition Institute, Sichuan Agricultural University, Chengdu, China.
Objectives:
Tea polyphenol (TP) epigallo-catechin-3-gallate (EGCG) can alleviate vanadium (V) stress in laying hens; however, our understanding of the molecular mechanisms and proteomic changes occurring in the egg albumen remains limited. The aim of the present study is to better understand the response in layers under V challenge and mechanism of EGCG detoxification.
Method:
We divided 120 layers into four treatments in the absence and presence of 130 mg/kg EGCG, supplemented with either 0 or 5 mg/kg V.
Results:
The Haugh unit (HU) was decreased and the apoptosis rate of magnum and V residual in egg was increased by the effect of vanadium and EGCG alleviated the detrimental effect in HU and apoptosis rate induced by vanadium (interactive effect, P < 0.05). In all, 379 proteins were identified and 28 differential proteins were observed with and without EGCG and V. Eight proteins, which respond to stress stimuli (five immune response proteins [F1P3B2, P21760, A2N881, F2Z4L6, and P02789], and one cell redox homeostasis protein [Q5F472] were presented in the albumen of laying hens with EGCG administration. Proteins involved in heavy metal binding (E1C5J4) and cell proliferation (F1NX05 and E1BT2) also were changed in EGCG-treated albumen.
Conclusion:
The detoxification mechanism of EGCG under V stress may act through regulating metal-binding mediation, cell proliferation, and immune function-related proteins.
