Drying and denaturation characteristics of α-LACTALBUMIN, β-lactoglobulin, and bovine serum albumin in a convective drying process
- Authors: Haque, M. Amdadul , Aldred, Peter , Chen, Jie , Barrow, Colin , Adhikari, Benu
- Date: 2014
- Type: Text , Journal article
- Relation: Journal of Agricultural and Food Chemistry Vol. 62, no. 20 (2014), p. 4695-4706
- Full Text: false
- Reviewed:
- Description: Drying and denaturation kinetics of aqueous droplets of α-lactalbumin (α-lac), β-lactoglobulin (β-lg), and bovine serum albumin (BSA) were measured in a convective drying environment. Single droplets having an initial droplet diameter of 2 ± 0.1 mm and containing 10% (w/v) protein concentration were dried using conditioned air (65 and 80 °C, 2-3% RH, 0.5 m/s velocity) for 600 s. The denaturation of these proteins was measured by using reversed-phase HPLC. At the end of 600 s of drying 13.3 and 19.4% α-lac was found to be lost due to denaturation at 65 and 80 °C, respectively. Up to 31.0% of β-lg was found to be denatured, whereas BSA was not found to be significantly (p > 0.05) denatured in these drying conditions. The formation and strength of skin and the associated morphological features were found to be linked with the degree of denaturation of these proteins. The secondary structure of these proteins was significantly (p < 0.05) affected and altered by the drying stresses. The β-sheet and random coil contents were increased in α-lac by 6.5 and 4.0%, respectively, whereas the α-helix and β-turn contents decreased by 5.5 and 5.0%, respectively. The β-sheet and random coil contents in β-lg were increased by 7.5 and 2.0%, respectively, whereas the α-helix and β-turn contents decreased by 3.5 and 6.0%, respectively. In the case of BSA the β-sheet, α-helix, and random coil contents were found to increase, whereas the β-turn content decreased. © 2014 American Chemical Society.
Physicochemical and functional properties of lentil protein isolates prepared by different drying methods
- Authors: Joshi, Matina , Adhikari, Benu , Aldred, Peter , Panozzo, Joe , Kasapis, Stefan
- Date: 2011
- Type: Text , Journal article
- Relation: Food Chemistry Vol. 129, no. 4 (2011), p. 1513-1522
- Full Text: false
- Reviewed:
- Description: Lentil protein isolate (LPI) extract was converted into powder by freeze drying, spray drying and vacuum drying. Differences in particle size distribution, protein subunit composition and colour and surface morphology were observed amongst the three drying methods. Spray and freeze-dried LPI powders exhibited higher solubility (81% and 78%, respectively) compared to vacuum dried powders (50%). The spray dried powders showed a low water absorption capacity (0.43 ± 0.02 g/g) compared to freeze (0.48 ± 0.02 g/g) and vacuum-dried (0.47 ± 0.01 g/g) LPI powders. Spray and freeze-dried powders displayed better gelation ability and higher gel strength, compared to vacuum-dried powder. Both spray and freeze-dried gels showed typical viscoelastic gel characteristics, with G′ dominating over G″ and very low loss tangent. The holding time required for gelation of vacuum dried powder at 90 °C was significantly longer, compared to spray and freeze dried powders. Hence, drying methods used for preparation of lentil protein isolate powders can affect physicochemical and associated functional properties. © 2011 Elsevier Ltd. All rights reserved.
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.