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Updated: Feb 10, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Formation and characterization of peptides in egg white during storage at ambient temperature
Meiyu Liu1, Wenlin Yu2, Fazheng Ren3
1College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, PR China; College of Life Science and Food Engineering, Hebei University of Engineering, Handan 056021, PR China; Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, AB T6G 2P5, Canada.
Abstract:
Egg white thinning during ambient storage is a well-known phenomenon. The objective of the study was to characterize the formation of peptides <10 kDa in egg white during storage at room temperature. The results indicated that the content of peptides in the egg white fraction of <10 kDa increased gradually. Similar but a faster trend was observed for the fraction of <3 kDa. Gallin, also called ovodefensin (∼7 kDa), was the main component in 10-3 kDa egg white fraction, which rapidly degraded and disappeared at 28 d of storage. Mass spectrometry analysis of <3 kDa fraction identified 6 peptide fragments from ovotransferrin and 11 peptides from ovomucin. Ovodefensin, ovotransferrin and ovomucin are the major innate components of egg defense; thus the degradation of these proteins during storage contributes to egg white thinning and increased susceptibility to bacterial contamination. This study provides the insights on the molecular mechanism of egg deterioration during prolonged ambient storage.
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