Forces involved in freeze-induced egg yolk gelation: Effects of various bond dissociation reagents on gel properties and protein structure changes.

Urea, sodium dodecyl sulfate (SDS) and β-mercaptoethanol (2-ME) were used to monitor the roles of hydrogen bonds, hydrophobic interactions and disulfide bonds in frozen egg yolk. Yolk samples were prepared with a denaturant, and the textural characteristics, turbidity properties, protein patterns and structures were analysed. The results showed that SDS or 2-ME addition to egg yolk promoted its turbidity and texture properties, but urea changed the turbidity differently. SDS-PAGE results showed that yolk protein patterns with urea slightly reduced the amount of high molecular weight substances, whereas SDS and 2-ME addition increased the amount. ATR-FTIR spectroscopy revealed that the protein secondary structures changed from ordered structures to random coils. The texture properties were correlated with the protein secondary structure, especially β-sheets and β-turns. Thus, the three bond dissociation reagents induced protein denaturation. Hydrogen bonds were the critical force affecting frozen egg yolk gelation, followed by hydrophobic interactions and disulfide bonds.