Abstract
Denaturation of glycinin by urea and guanidine hydrochloride (GdnHC1) has been studied at 30° by viscosity and circular dichroism (CD) measurements. The kinetics of denaturation by 8M urea at 20, 30, 40 and 50°, and by 6M GdnHC1 at 20° have been measured by monitoring the increase in absorbance at 287 nm as a function of time. Viscosity increased with denaturant concentration and reached maximum value of 28 mL/g at 6M GdnHC1 and 7M urea. The (negative) molar ellipticity values in the region 250–200 nm decreased with increase in denaturant concentration. Analysis of viscosity and CD data indicated that both sets of data fitted the same curve of fd (fraction of protein denatured) versus denaturant concentration. The kinetic data followed first order reaction kinetics, These suggest that denaturation of glycinin by urea/GdnHC1 is a two‐state process and follows the same pattern as that of globular proteins.
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