Abstract
Fourier transform near-infrared (FT-NIR) spectra have been measured for bovine serum albumin (BSA) in an aqueous solution (pH 6.8) with a concentration of 5.0 wt% over a temperature range of 45-85 degrees C. Not only conventional spectral analysis methods, such as second-derivative spectra and difference spectra, but also chemometrics, such as principal component analysis (PCA) and evolving factor analysis (EFA), have been employed to analyze the temperature-dependent NIR spectra in the 7500-5500 and 4900-4200 cm-1 regions of the BSA aqueous solution. Intensity changes of bands in the 7200-6600 cm-1 and 4650-4500 cm-1 regions in the difference spectra indicate variations of the hydration and secondary structure of BSA in the aqueous solution, respectively. The plot of a band intensity at 7080 cm-1 in the different spectra shows a clear turning point at 63 degrees C, revealing that a significant change in the hydration occurs at about 63 degrees C. The forward and backward eigenvalues (EVs) from EFA suggest that marked changes in the hydration and secondary structure of BSA take place in the temperature ranges of 61-65 degrees C and 59-63 degrees C, respectively. In addition, the temperature of 71 degrees C marked in the EFA plots may correspond to the onset temperature of increase in the intermolecular beta-sheet structure.
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