Unexpected high pressure effects on the structural properties of condensed whey protein systems
- Authors: Dissanayake, Muditha , Kasapis, Stefan , Chaudhary, Vinita , Adhikari, Benu , Palmer, Martin , Meurer, Barbara
- Date: 2012
- Type: Text , Journal article
- Relation: Biopolymers Vol. 97, no. 12 (2012), p. 963-973
- Full Text: false
- Reviewed:
- Description: We show that application of high hydrostatic pressure (600 MPa for 15 min) on condensed whey protein (WP) systems (e.g., 80% w/w solids content) results in unexpected structure-function behavior when compared with conventional thermal treatment. Unraveling the relaxation properties in first-order thermodynamic transitions, the manifestation of glass transition phenomena and the preservation of native conformation in condensed preparations were recorded using small-deformation dynamic oscillation in shear, modulated differential scanning calorimetry, and infrared spectroscopy. Informed temperature application results in the formation of continuous networks at the denaturation temperature, which undergo vitrification at subzero temperatures. In contrast, high-pressure-treated WPs resist physicochemical denaturation, hence preserving the native conformation of secondary and tertiary structures. This was rationalized on the basis of a critical concentration threshold where transfer of water molecules to nonpolar residues in the protein interior is minimized because of low moisture content and restricted molecular mobility. The physical state and morphology of these high-solid preparations were further examined by the combined framework of reduced variables and Williams, Landel, and Ferry equation/free volume theory. Theoretical treatment of experimental observations unveils the dynamic range of the mechanical manifestation of the glass transition region in samples subjected to heat or pressure. In addition to preserving native conformation, WPs subjected to high pressure form glassy systems at parity with the structural functionality of the thermally treated counterparts. © 2012 Wiley Periodicals, Inc.
Hydrostatic pressure effects on the structural properties of condensed whey protein/lactose systems
- Authors: Dissanayake, Muditha , Kasapis, Stefan , George, Paul , Adhikari, Benu , Palmer, Martin , Meurer, Barbara
- Date: 2013
- Type: Text , Journal article
- Relation: Food Hydrocolloids Vol. 30, no. 2 (March 2013), p. 632-640
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- Reviewed:
- Description: Hydrostatic pressure effects on whey protein/lactose mixtures were recorded with subsequent analysis of their structural, molecular and glass transition properties in comparison to thermal effects at atmospheric pressure. Experimental techniques used were small deformation dynamic oscillation in shear, modulated differential scanning calorimetry, Fourier transform infrared spectroscopy, and theoretical modelling of glass transition phenomena. Levels of solids ranged from 30 to 80% (w/w) in formulations with a protein/co-solute ratio of four-to-one. Addition of lactose protects the secondary conformation of the protein under application of high hydrostatic pressure. Nevertheless, pressurized protein systems are able to form three-dimensional structures due to the reduction in polymeric free volume and the development of an efficient friction coefficient amongst tightly packed particles. Systems can be seen as developing a "molten globular state", where the structural knots of pressure-treated networks remain in the native conformation but achieve intermolecular cross-linking owing to frictional contact. Furthermore, pressure treated assemblies of condensed whey protein preparations could match the viscoelasticity of the thermally treated counterparts upon cooling below ambient temperatures. That allowed examination of the physical state and morphology of a condensed preparation at 80% solids by the combined framework of reduced variables and free volume theory thus affording derivation of glass transition temperatures for pressurized and atmospheric samples. (C) 2012 Published by Elsevier Ltd.