In this study, we investigated thermal properties of native ovalbumin (OVA) solutions as well as gels prepared by high temperature heat treatment using differential scanning calorimetry (DSC). The denaturation temperature,
td, and the heat of denaturation, Δ
H, of native OVA in water were found to take a constant value of 75.0°C and 890kJ mol
-1 for OVA concentration
C ranging from 5 to 58 wt%, respectively, whereas rising of
td and a decrease in Δ
H occurred with a further increase in
C. Assumption of the closest packing for OVA with bound water at
C=58wt% gives that the amount of bound water on the OVA surface is 0.36g per g of OVA with
C < 58wt% and decreases with increasing
C. The thickness of the surface layer is then estimated as 0.36nm for OVA sphere with the diameter of 5.6nm. Aqueous OVA solutions with
C≥10wt% showed three exothermic peaks at around 140°C, 170°C and 220°C, which may be related to transformation from the randomly aggregated state of OVA to stable gel network, to breakage of the S-S bond and to degradation of the protein itself, respectively. Circular dichroism measurement revealed that a decrease in α-helix content at around 80°C was followed by decreases in the β-sheet and the β-turn contents at higher temperature, which indicate that changes in the secondary structure of OVA play a deterministic role for gel formation in the temperature range of 100-140°C and for subsequent transformation to the random coil form before degradation starts at 200°C. Two organic solvents, glycerin and ethylene glycol, and their water mixtures were used as solvent to study the effect of hydrophobicity on thermal behaviour of OVA. Quite complicated changes in
td and Δ
H with mixing ratio were observed, and ethylene glycol was found to interact more strongly with native OVA than glycerin did.
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