Potential of capillary electrophoresis with wavelength-resolved fluorescence detection for protein unfolding studies using beta-lactoglobulin B as a test compound

Capillary electrophoresis (CE) with wavelength-resolved fluorescence detection (wrFlu) was evaluated for the study of protein unfolding using non-reduced and reduced β-lactoglobulin B (β-LGB) as model compounds. Protein unfolding was achieved by incubation in sodium phosphate (pH 3.0) containing increasing concentrations of urea (0-7.1 M). CE-wrFlu was performed using the incubation media as background electrolytes (BGEs). At low urea concentrations (0-3.1 M), CE-wrFlu analysis of non-reduced β-LGB showed a single peak with a maximum emission wavelength (λ