An isothermal titration calorimetry study of phytate binding to lysozyme

被引:30
作者
Darby, Samuel J. [1 ]
Platts, Lauren [1 ]
Daniel, Matthew S. [1 ]
Cowieson, Aaron J. [2 ]
Falconer, Robert J. [1 ]
机构
[1] Univ Sheffield, ChELSI Inst, Dept Chem & Biol Engn, Sheffield S1 3JD, S Yorkshire, England
[2] DSM Nutr Prod, Kaiseraugst, Switzerland
基金
英国生物技术与生命科学研究理事会;
关键词
Allostery; Cooperative binding; ITC; Phytase; Digestion; DRINKING-WATER TEMPERATURE; PHYTIC ACID; AQUEOUS-SOLUTION; HEAT-CAPACITY; P-31; NMR; PROTEINS; IONIZATION; FLAVAN-3-OLS; PERFORMANCE; STABILITY;
D O I
10.1007/s10973-016-5487-6
中图分类号
O414.1 [热力学];
学科分类号
摘要
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.
引用
收藏
页码:1201 / 1208
页数:8
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