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.
The effects of proteins and low molecular weight surfactants on spray drying of model sugar-rich foods: Powder production and characterisation
- Authors: Jayasundera, Mithila , Adhikari, Benu , Adhikari, Raju , Aldred, Peter
- Date: 2011
- Type: Text , Journal article
- Relation: Journal of Food Engineering Vol. 104, no. 2 (2011), p. 259-271
- Full Text: false
- Reviewed:
- Description: The effects of proteins and low molecular weight surfactants (LMS) on spray drying and powder characteristics of model sugar-rich foods have been studied. Fructose and sucrose were selected as model sugar-rich foods and sodium caseinate (NaCas) was selected as a model protein. Sodium stearoyl lactylate (SSL) and Polysorbate 80 (Tween-80) were chosen as model ionic and non-ionic low molecular weight surfactants. The feed solutions for spray drying had 25% solid concentration in all. To achieve identical powder recoveries of the order of 80% much higher NaCas:fructose ratio (30:70) was required compared to NaCas:sucrose ratio (0.5:99.5) which corresponded to 7.89% and 0.13% of sodium caseinate (initial bulk concentration), respectively. There was no change in powder recovery when the SSL concentration was increased from 0.01% to 0.05% in fructose-NaCas-SSL solution and also addition of 0.01% Tween-80 into fructose-NaCas solution did not affect the powder recovery (76.7 ± 2.3%), however, it was slightly affected with the increase of Tween-80 to 0.05% (69.0 ± 1.9%). At NaCas concentration above critical micelle concentration of NaCas (3% w/w), the presence of up to 0.05% low molecular weight surfactants had either no effect or minimal effect on the surface coverage of the droplets/particles and also on the powder recovery depending on the nature of the low molecular weight surfactants. The surface protein coverage and the recovery of the powder in sucrose-protein systems were very sensitive in the presence of low molecular weight surfactants due to being below the critical micelle concentration of NaCas. SSL displaced 2.0% and 29.3% of proteins from the droplet surface of sucrose-NaCas-SSL, respectively, when its concentration was varied from 0.01% to 0.05% thereby reducing the powder recovery from 75.5% to 30%. The addition of 0.01% Tween-80 in sucrose-NaCas solution resulted in a 48.2 ± 1.5% reduction in powder recovery and at 0.05% concentration, it displaced a substantial amount of NaCas from the droplet surface and no powder was recovered. These phenomena are explained on the basis of surface-glass transition temperature, dynamic surface tension, nature of surfactants and glass transition temperature of sugars used. X-ray diffraction and scanning electron microscopy results showed that the powders of sucrose-NaCas, sucrose-NaCas with 0.01% SSL and all powders of fructose were amorphous. © 2010 Elsevier Ltd. All rights reserved.