N-glycosylation and gelling properties of ovomucin from egg white
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Abstract
Ovomucin is a bioactive egg white glycoprotein responsible for its gel-like properties and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin and a carbohydrate-poor α-ovomucin. N-glycosylation of ovomucin was studied by nano LC ESI-MS, MS/MS and MALDI MS. Both proteins were N-glycosylated and site-occupancy of 18 potential N-glycosylation sites in α-ovomucin and two sites in β-ovomucin was determined. N-glycans of α-ovomucin were bisected complex-type glycans, while GlcNAc6Man3 was the most abundant glycan. In the second part, rheology and microstructure of aqueous ovomucin dispersions were studied. Ovomucin formed a fibrous network with weak gel properties in distilled water at room temperature and shear thinning behaviour, suggesting that ovomucin can be used as a thickener and stabilizer in various applications. In addition, influence of salt on ovomucin gel and its isoelectric point was determined.