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.
Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes
- Authors: Haque, M. Amdadul , Aldred, Peter , Chen, Jie , Barrow, Colin , Adhikari, Benu
- Date: 2013
- Type: Text , Journal article
- Relation: Food Chemistry Vol. 141, no. 2 (2013), p. 702-711
- Full Text: false
- Reviewed:
- Description: The extent and nature of denaturation of whey protein isolate (WPI) in convective air drying environments was measured and analysed using single droplet drying. A custom-built, single droplet drying instrument was used for this purpose. Single droplets having 5. ±. 0.1. μl volume (initial droplet diameter 1.5. ±. 0.1. mm) containing 10% (w/v) WPI were dried at air temperatures of 45, 65 and 80. °C for 600. s at constant air velocity of 0.5. m/s. The extent and nature of denaturation of WPI in isothermal heat treatment processes was measured at 65 and 80. °C for 600. s and compared with those obtained from convective air drying. The extent of denaturation of WPI in a high hydrostatic pressure environment (600. MPa for 600. s) was also determined. The results showed that at the end of 600. s of convective drying at 65. °C the denaturation of WPI was 68.3%, while it was only 10.8% during isothermal heat treatment at the same medium temperature. When the medium temperature was maintained at 80. °C, the denaturation loss of WPI was 90.0% and 68.7% during isothermal heat treatment and convective drying, respectively. The bovine serum albumin (BSA) fraction of WPI was found to be more stable in the convective drying conditions than
- Description: 2003011092