ABSTRACTThe enthalpy of denaturation (ΔH) and surface properties of proteins were related to elucidate the mechanisms of foaming and emulsifying properties by using various heated egg white proteins in the dry state. Foaming and emulsifying properties of all sample proteins were greatly increased with a decrease in the enthalpy of denaturation as determined by differential scanning calorimetry analysis. In plots, foaming and emulsifying properties correlated linearly with ΔH values for various dry‐heated egg white proteins. Thus, the enthalpy of denaturation of proteins seemed to be a significant structural factor governing surface functional propert
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