A Comprehensive Identification of Chicken Egg White Phosphoproteomics Based on a Novel Digestion Approach

Abstract

There are plenty of phosphoproteins in chicken egg white (CEW), which are of great significance for the biological activity and function of CEW. In this study, phosphorylated proteins in CEW were identified and analyzed based on two digestion strategies (trypsin and trypsin/glutamyl endoproteinase). Besides, the enrichment strategy of immobilized metal affinity chromatography was used, and phosphopeptides were identified by nano liquid chromatography/tandem mass spectrometry. A total of 189 phosphosites mapped onto 166 phosphopeptides corresponding to 96 phosphoproteins were identified. Gene ontology analysis suggested that these phosphoproteins of CEW mainly participated in biological processes such as "cell process", "biological regulation", and "response to stimulus". Moreover, the phosphoproteins of CEW were involved in molecular functions, primarily including "binding" and "catalytic activity". On the basis of the available literature, the research was the first comprehensive identification of chicken egg white phosphoproteins. This study further enriched the identification of phosphoproteins in CEW and laid a foundation for the subsequent study of phosphoproteins.

Phosphoproteomics Profile of Chicken Cecum in the Response to Salmonella enterica Serovar Enteritidis Inoculation

“…Phosphoproteomic analysis is a powerful technique for investigating phosphoprotein expression patterns, and has been used for chickens in several studies [13,19,20]. The regulation mechanism of chicken cecum infected with S. Enteritidis is still being investigated; however, post-translational modifications, especially phosphorylation, might play an important role.…”

Antimicrobial Proteins and Peptides in Avian Eggshell: Structural Diversity and Potential Roles in Biomineralization

“…Members of this family, such as mouse and human latexin, adopt a cystatin-like fold similar to that found in chicken cystatin ( Figure 6A ). OCX-32 contains two cystatin-like units ( Figure 6B ) and is phosphorylated at serine residues 261 and 268 ( 129 , 140 ). The distribution of electrostatic charges reveals two domains, one cationic domain (N-ter domain) and one rather acidic domain (C-ter domain) ( Figure 6B , right panel), which may be involved in distinct interactions with eggshell components (other proteins, glycosaminoglycans, mineral phase).…”

Characterization of the interactions between Fulvic acid and Trypsin with Spectroscopic and Molecular Docking technology

“…Trypsin (TRP) primarily functions as a digestive enzyme in the human body, exerting inhibitory effects on the activation of chymotrypsinogen, carboxypeptidase, phospholipase, and other precursor enzymes while actively participating in enzymatic regulation. [15] TRP is the most specific protease with an indispensable role in human physiology. [16] During the process of decomposition and absorption, drugs inevitably interact with various proteases or other crucial proteins, thereby impacting protein structure and function.…”

“…Trypsin (TRP) primarily functions as a digestive enzyme in the human body, exerting inhibitory effects on the activation of chymotrypsinogen, carboxypeptidase, phospholipase, and other precursor enzymes while actively participating in enzymatic regulation [15] . TRP is the most specific protease with an indispensable role in human physiology [16] .…”