Drying and denaturation characteristics of α-lactalbumin, β-lactoglobulin, and bovine serum albumin in a convective drying process Haque,MA, Aldred,P, Chen,J, Barrow,C and Adhikari,B 2014, Drying and denaturation characteristics of α-lactalbumin, β-lactoglobulin, and bovine serum albumin in a convective drying process, Journal of Agricultural and Food Chemistry, vol. 62, no. 20, pp. 4695-4706, doi: 10.1021/jf405603c. Attached Files Name Description MIMEType Size Downloads Title Drying and denaturation characteristics of α-lactalbumin, β-lactoglobulin, and bovine serum albumin in a convective drying process Author(s) Haque,MA Aldred,P Chen,J Barrow,C orcid.org/0000-0002-2153-7267 Adhikari,B Journal name Journal of Agricultural and Food Chemistry Volume number 62 Issue number 20 Start page 4695 End page 4706 Total pages 12 Publisher American Chemical Society Place of publication Washington, DC Publication date 2014-05-21 ISSN 1520-5118 Keyword(s) bovine serum albumin drying morphology single droplet α-helix α-lactalbumin and β-lactoglobulin denaturation β-sheet β-turn Science & Technology Life Sciences & Biomedicine Physical Sciences Agriculture, Multidisciplinary Chemistry, Applied Food Science & Technology Agriculture Chemistry alpha-lactalbumin and beta-lactoglobulin denaturation beta-sheet beta-turn alpha-helix TRANSFORM INFRARED-SPECTROSCOPY SECONDARY STRUCTURE PROTEIN CONFORMATION SELF-DECONVOLUTION SURFACE STICKINESS HEAT-TREATMENT WHEY PROTEINS MILK POWDER AMIDE-I Animals Summary 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. Language eng DOI 10.1021/jf405603c Field of Research 090802 Food Engineering Socio Economic Objective 860105 Nutraceuticals and Functional Foods HERDC Research category C1 Refereed article in a scholarly journal ERA Research output type C Journal article Copyright notice ©2014, American Chemical Society Persistent URL http://hdl.handle.net/10536/DRO/DU:30070406 Document type: Journal Article Collections: Faculty of Science, Engineering and Built Environment School of Life and Environmental Sciences Related Links Link Description Connect to Elements publication management system Go to link with your DU access privileges   Connect to published version Go to link with your DU access privileges   Author URL Go to link with your DU access privileges     Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Versions Version Filter Type Tue, 10 Mar 2015, 10:39:37 EST Wed, 11 Mar 2015, 04:01:42 EST Wed, 11 Mar 2015, 07:13:30 EST Wed, 25 Mar 2015, 15:14:38 EST Wed, 25 Mar 2015, 15:16:55 EST Tue, 31 Mar 2015, 05:08:04 EST Tue, 31 Mar 2015, 09:38:08 EST Tue, 31 Mar 2015, 09:44:36 EST Filtered Full Citation counts:   Cited 21 times in TR Web of Science Cited 21 times in Scopus Search Google Scholar Access Statistics: 638 Abstract Views, 3 File Downloads  -  Detailed Statistics Created: Tue, 10 Mar 2015, 10:39:37 EST