NDLI: An isothermal titration calorimetry study of phytate binding to lysozyme : A multisite electrostatic binding reaction

Content Provider	Springer Nature Link
Author	Darby, Samuel J. Platts, Lauren Daniel, Matthew S. Cowieson, Aaron J. Falconer, Robert J.
Copyright Year	2016
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.
Starting Page	1201
Ending Page	1208
Page Count	8
File Format	PDF
ISSN	13886150
Journal	Journal of thermal analysis
Volume Number	127
Issue Number	2
e-ISSN	15882926
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-04-29
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Allostery Cooperative binding ITC Phytase Digestion Physical Chemistry Analytical Chemistry Polymer Sciences Inorganic Chemistry Measurement Science and Instrumentation
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry Condensed Matter Physics

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