Molecular structure modification of ovalbumin through controlled glycosylation with dextran for its emulsibility improvement

Ovalbumin (OVA) is a high nutritious protein, but the poor emulsibility limited its application. The present study glycosylated OVA with dextran (Dex) by controlled wetheating (60–90 °C for 3 h). Temperature was an inductive factor for glycosylation degree (DG and browning intensity), and higher temperature could accelerate the reaction. Variations in molecular structure of OVA were analyzed by SDS-PAGE, FTIR, fluorescence spectroscopy and UV spectroscopy, which verified successes in the generation of glycoconjugate with more flexible structure. Emulsifying activity index (EAI) and emulsion stability index (ESI) for the emulsion of OVA-Dex glycoconjugates were significantly enhanced with the increasing of glycosylation temperature. Moreover, confocal laser scanning results revealed that the emulsion exhibited smaller size and more uniform distribution, and slower transmission profiles were checked by LUMiSizer centrifugal analysis as well, confirming the emulsibility improvement of OVA. Thus, controlled glycosylation reaction is an available method to improve the emulsifying properties of OVA.