http://researchonline.federation.edu.au/vital/access/manager/Index ${session.getAttribute("locale")} 5 Drying and denaturation characteristics of α-LACTALBUMIN, β-lactoglobulin, and bovine serum albumin in a convective drying process http://researchonline.federation.edu.au/vital/access/manager/Repository/vital:12771 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.]]> Tue 03 Jul 2018 11:28:03 AEST ]]> Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes http://researchonline.federation.edu.au/vital/access/manager/Repository/vital:5082 Fri 26 Jul 2019 13:50:02 AEST ]]>