Abstract
The thermal denaturation process of a model protein, bovine β-lactoglobulin, was analyzed using capillary zone electrophoresis (CZE). For this purpose, a commercial CE apparatus was improved, allowing efficient control and accurate measurement of the temperature up to 95°C. Under various pH conditions, transition temperature ( T m), enthalpy change (Δ H) and entropy change (Δ S) associated with the thermal denaturation were determined. Moreover, the technique is unique in its ability to estimate the heat capacity change (Δ C p). This work shows that CZE, performed even when electroosmotic flow occurs, is an innovative approach for determining the stability curves of proteins. Accordingly, CZE is a powerful tool to study protein unfolding/folding quickly and with minimal sample requirements.
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