Identification and comparative proteomic study of quail and duck egg white protein using 2-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry analysis

Abstract

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.

Comparative proteomic analysis of chicken, duck, and quail egg yolks

“…As a trypsin and chymotrypsin inhibitor, [37] ovoinhibitor has been found in the egg white of chicken, quail, and ostrich. [11] Its deficiency in duck egg white may suggest weaker inhibition of endogenous protease activity and shorter storage period than those of chicken and quail eggs.…”

“…As three most consumed avian eggs all over the world, chicken, quail, and duck eggs might have different egg protein patterns due to the adaptation under varied environments and evolution. According to the phylogenetic analysis with whole mitochondrial genome [10] and egg white proteome [11] than duck. These data implied that the protein patterns of these three avian egg yolks were different, which might be of significant importance in biology.…”

Comparative study on the effect of duck and hen egg albumens on proteolysis and gel property of sardine surimi

“…which were able to inhibit serine protease. [2] Hu et al [13] reported that duck ovostatin (ovamacroglobulin) is capable of inhibiting serine protease as well as metalloprotease, while chicken ovostatin inhibits only metalloprotease. Moreover, Shah and Khan [14] proved that duck ovomucoid effectively stabilised salmon calcitonin against hydrolysis mediated by three proteases including trypsin, α-chymotrypsin and elastase.…”

“…Protein contents of lyophilised albumen from duck and quail eggs were higher than that of hen egg. [12,13] Moreover, ovomucoid from duck and hen albumen also showed different protease inhibitory activity in protection of salmon calcitonin breakdown by serine proteases. [14] In general, hen albumen has been commonly manufactured into different forms, such as powder, pasteurised liquid albumen, etc.…”

Identification of Ophiocordyceps sinensis and Its Artificially Cultured Ophiocordyceps Mycelia by Ultra-Performance Liquid Chromatography/Orbitrap Fusion Mass Spectrometry and Chemometrics

“…and, to the best of our knowledge, have rarely been studied and reported [40]. Biological mass spectrometry has been developed as an efficient method for proteomic analysis that exhibits superior mass accuracy and ultra-high resolution, and employs a segmented quadruple mass filter with improved selectivity and ion transmissibility [38,39,41,42,43,44,45,46]. However, for a specific genus, there is only limited data available to characterize the fungal protein.…”