TY  - JOUR
A1  - Baier, Daniel
A1  - Purschke, Benedict
A1  - Schmitt, Christophe
A1  - Rawel, Harshadrai Manilal
A1  - Knorr, Dietrich
T1  - Effect of high pressure - low temperature treatments on structural characteristics of whey proteins and micellar caseins
T2  - Food chemistry
N2  - 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 degrees C and -35 degrees 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 beta-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. (C) 2015 Elsevier Ltd. All rights reserved.
KW  - High pressure - low temperature treatments
KW  - Whey proteins
KW  - Micellar caseins
KW  - Structural changes
Y1  - 2015
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/38446
SN  - 0308-8146
SN  - 1873-7072
VL  - 187
SP  - 354
EP  - 363
PB  - Elsevier
CY  - Oxford
ER  -