Abstract
The changes induced by ethanol treatments at different concentrations (20%, 40%, 60%, and 80%, v/v) on the structural, morphological and functional properties of native whey protein isolates (WPI) were investigated. The results showed that the secondary and tertiary structures of native WPI were clearly altered with ethanol treatment. The resulting molecular unfolding and subsequent aggregation was due to the formation of disulfide bonds and intramolecular hydrogen bonds, as well as hydrophobic interactions. Morphological observations revealed that ethanol treated WPI (E-WPI) had larger irregular block-shaped structures. Moreover, E-WPI prepared with an intermediate ethanol concentration (40% in our study) showed the highest emulsifying activity, emulsifying stability, foaming capacity, and surface hydrophobicity.
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