Effect of high pressure--low temperature treatments on structural characteristics of whey proteins and micellar caseins.

Daniel Baier, Benedict Purschke, Christophe Schmitt, Harshadrai M Rawel, Dietrich Knorr

Index: Food Chem. 187 , 354-63, (2015)

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Abstract

In this study, structural changes in micellar caseins and whey proteins due to high pressure--low temperature treatments (HPLT) were investigated and compared to changes caused by high pressure treatments at room temperature. Whey protein isolate (WPI) solutions as well as micellar casein (MC) dispersions and mixtures were treated at 500 MPa (pH 7.0 and 5.8) at room temperature, -15 °C and -35 °C. Surface hydrophobicity and accessible thiol groups remained nearly unchanged after HPLT treatments whereas HP treatments at room temperature caused an unfolding of the WPI, resulting in an increase in surface hydrophobicity and exposure of the thiol groups. For HPLT treatments, distinct changes in the secondary structure (increase in the amount of β-sheets) were observed while the tertiary structure remained unchanged. Large flocs, stabilized by hydrophobic interactions and hydrogen bonds, were formed in casein containing samples due to HPLT treatments. Depending on the pH and the applied HPLT treatment parameters, these interactions differed significantly from the interactions determined in native micelles.Copyright © 2015 Elsevier Ltd. All rights reserved.