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Thus, dynamic high-pressure treatment did not influence equilibrium interfacial tension but enhanced adsorption kinetic. This could be explained by whey protein particle size decrease leading both to an increase in mobility in the bulk phase and an unmasking of hydrophobic groups. This is in accordance with results found by Zhang, Dalgleish, & Goff (2004) who assumed that the major thermodynamic driving force for protein adsorption at an air¨Cwater interface is the mean residue hydrophobicity. This assumption is confirmed since native WPI solution displayed higher adsorption kinetic when filtered (0.45 mm), while treated WPI solutions (300MPa) kept the same adsorption rate (data not shown).
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Temperature of polypeptide inverse temperature transition depends on mean residue hydrophobicity
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