Abstract
Heat-induced changes in the physicochemical properties of whey protein isolate (WPI) have been studied. WPI (5%) heated at 70 o C underwent rapid conformational changes within 1 min. The aperiodic structure content increased primarily at the cost of β-sheet structure. The hydrophobic character, as measured by changes in the pH-solubility profile and the solubility profile at pH 4.6 in NaCl solutions, of the protein surface increased. However, the surface hydrophobicity, as measured by the cis-parinaric acid binding method, decreased. In contrast, WPI (9%) heated at 90 o C did not exhibit significant changes in the secondary structure content
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