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A proteomic study of egg white proteins from 2 major poultry species, namely quail (Coturnix coturnix) and duck (Anas platyrhynchos), was performed with comparison to those of chicken (Gallus gallus) through 2-dimensional polyacrylamide gel electrophoresis (2-DE) analysis. By using matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry (MALDI-TOF MS/MS), 29 protein spots representing 10 different kinds of proteins as well as 17 protein spots designating 9 proteins were successfully identified in quail and duck egg white, respectively. This report suggested a closer relationship between quail and chicken egg white proteome patterns, whereas the duck egg white protein distribution on the 2-DE map was more distinct. In duck egg white, some well-known major proteins, such as ovomucoid, clusterin, extracellular fatty acid-binding protein precursor (ex-FABP), and prostaglandin D2 synthase (PG D2 synthase), were not detected, while two major protein spots identified as “deleted in malignant brain tumors 1” protein (DMBT1) and vitellogenin-2 were found specific to duck in the corresponding range on the 2-DE gel map. These interspecies diversities may be associated with the egg white protein functions in cell defense or regulating/supporting the embryonic development to adapt to the inhabiting environment or reproduction demand during long-term evolution. The findings of this work will give insight into the advantages involved in the application on egg white proteins from various egg sources, which may present novel beneficial properties in the food industry or related to human health.

A comparative analysis of egg yolk proteome of three major poultry species, namely, chicken, duck, and quail, was carried out with two-dimensional (2D) gel electrophoresis patterns and matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry. Proteins identified from these three poultry species shared high degrees of sequence and structure homology, which might be related to the bird's adaptability under different environmental stresses. Few specific proteins were found in this study. Comparative 2D gel electrophoresis patterns of chicken, duck, and quail revealed that some protein-specific regions on gels could be used for authentic identification of poultry eggs. These findings could provide a fundamental understanding of different poultry egg protein profiles and showed us some new sights in egg yolk nutrients related to certain properties and functions.ARTICLE HISTORY

Supercritical carbon dioxide (SC-CO2) dyeing for the polyethylene terephthalate (PET) and cotton fabric was implemented by a modified dynamic-recirculation apparatus that was successfully designed and constructed in our laboratory. This energy-efficient apparatus contains two horizontal dyeing vessels and equips the rotating warp beam. The circulating SC-CO2 fluid and revolving fabrics facilitate the uniform adsorption and quick uptake of dye molecules to the fabrics. Moreover, three dyes were synthesized and applied for dyeing fabric samples performed in mild conditions of 353.2 K and 18.0 MPa for 60 min in SC-CO2. Satisfactory and commercially acceptable products with reasonably good color uniformity, color strength and color fastness were obtained in dyeing experiments with this SC-CO2 apparatus. Color characteristics of the dyed PET and cotton fabrics such as the absorption and reflectance spectra were determined, and their surface morphologies were investigated by scanning electron microscopy.

It is likely that the increased degradation of protease inhibitors such as ovoinhibitor and α -macroglobulin-like protein 1-like during prolonged storage lead to an imbalance of protease and antiprotease in egg yolk, which may play a key role in the degradation of egg yolk proteins. These findings will provide an insight into the effects of storage on egg yolk protein changes and give a deeper understanding of the deteriorative process of chicken egg yolk. © 2016 Society of Chemical Industry.

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