The effects of high-intensity ultrasound on the structural and functional properties of alpha-Lactalbumin, beta-Lactoglobulin and their mixtures

Chandrapala, J, Zisu, B, Kentish, S and Ashokkumar, M 2012, 'The effects of high-intensity ultrasound on the structural and functional properties of alpha-Lactalbumin, beta-Lactoglobulin and their mixtures', Food Research International, vol. 48, no. 2, pp. 940-943.


Document type: Journal Article
Collection: Journal Articles

Title The effects of high-intensity ultrasound on the structural and functional properties of alpha-Lactalbumin, beta-Lactoglobulin and their mixtures
Author(s) Chandrapala, J
Zisu, B
Kentish, S
Ashokkumar, M
Year 2012
Journal name Food Research International
Volume number 48
Issue number 2
Start page 940
End page 943
Total pages 4
Publisher Elsevier
Abstract In this study, the structural and functional changes of pure and 3:1 mixtures of beta-Lactoglobulin (beta-LG) and alpha-Lactalbumin (alpha-LA), the most abundant whey proteins in milk were studied after sonication at 20 kHz (31 W) for up to 60 min. The reactive thiol content and surface hydrophobicity of pure beta-LG increased continuously during sonication, suggesting an unfolding of the dimer structure. Minor secondary and tertiary structural changes were also observed by circular dichroism. The alpha-LA protein appeared to be more strongly affected by sonication, with significant increases in surface hydrophobicity. The results suggest that sonication has a greater effect on alpha-LA than on beta-LG, which means that the properties of their mixture differ substantially from that of either protein in isolation.
Subject
Food Sciences
Keyword(s) beta-Lactoglobulin
alpha-Lactalbumin
Ultrasound
Denaturation
DOI - identifier 10.1016/j.foodres.2012.02.021
Copyright notice © 2012 Elsevier Ltd. All rights reserved.
ISSN 0963-9969
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