Quantitative N-glycoproteomic analysis of egg yolk powder during thermal processing

Abstract

The production of egg yolk powder often involves critical processes such as pasteurization and spray drying, however, these thermal processes will inevitably affect the functional properties of egg yolk (especially gelation and emulsification). The aim of this study was to elucidate the mechanism of the effect of pasteurized egg yolk (P-EY) and spray-dried egg yolk (SD-EY) on the functional properties through quantitative N-glycoproteomic. The results showed, compared with fresh egg yolk (F-EY), emulsifying property of mild heat-treated P-EY was slightly reduced while the gelation property did not undergo significant changes, whereas emulsifying activity (EAI) and gelation strength of vigorously heat-treated SD-EY were significantly reduced by 48.72 % and 35.73 %, respectively. During thermal processing in SD-EY, larger aggregate particles (particle size ∼10 um) were formed, and the surface hydrophobicity was reduced (93.0 %) and the zeta potential was enhanced (62.8 %). The results of quantitative N-glycoproteomic showed that 13 N-glycosylated proteins (APOB, vitellogenin, etc.) were down-regulated while only 2 N-glycosylated proteins were up-regulated; 21 N-glycosylation sites were down-regulated and 2 N-glycosylation sites were up-regulated in SD-EY, suggesting that covalent cross-linking of protein N-glycoproteins may have occurred in the process of spray-drying, which altered molecular physicochemical characteristics of the yolk solution that further affecting the processing properties of egg yolk.