Darby, S.J., Platts, L., Daniel, M.S. et al. (2 more authors) (2017) An isothermal titration calorimetry study of phytate binding to lysozyme: A multisite electrostatic binding reaction. Journal of Thermal Analysis and Calorimetry, 127 (2). pp. 1201-1208. ISSN 1388-6150
Abstract
Isothermal titration calorimetry (ITC) was used to detect phytate binding to the protein lysozyme. This binding interaction was driven by electrostatic interaction between the positively charged protein and negatively charged phytate. When two phytate molecules bind to the protein, the charge on the protein is neutralised and no further binding occurs. The stoichiometry of binding provided evidence of phytate–lysozyme complex formation that was temperature dependent, being most extensive at lower temperatures. The initial stage of phytate binding to lysozyme was less exothermic than later injections and had a stoichiometry of 0.5 at 313 K, which was interpreted as phytate crosslinking two lysozyme molecules with corresponding water displacement. ITC could make a valuable in vitro assay to understanding binding interactions and complex formation that normally occur in the stomach of monogastric animals and the relevance of drinking water temperature on the extent of phytate–protein interaction. Interpretation of ITC data in terms of cooperativity is also discussed.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © The Author(s) 2016. This article is published with open access at Springerlink.com |
Keywords: | Allostery; Cooperative binding; ITC; Phytase; Digestion |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Engineering (Sheffield) > Department of Chemical and Biological Engineering (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 05 Jul 2016 12:15 |
Last Modified: | 06 Mar 2017 15:52 |
Published Version: | http://dx.doi.org/10.1007/s10973-016-5487-6 |
Status: | Published |
Publisher: | Springer Verlag |
Refereed: | Yes |
Identification Number: | 10.1007/s10973-016-5487-6 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:101525 |