Abstract

Fourier transform infrared (FT-IR) spectra have been measured for defatted bovine serum albumin (BSA) in D<sub>2</sub>O with a concentration of 2.0 wt % over a temperature range of 26–90 °C and the corresponding difference spectra have been calculated by subtracting the contribution of D<sub>2</sub>O at the same temperature. Evolving factor analysis (EFA) by selecting two factors and three factors has been employed to analyze the temperature-dependent difference IR spectra in the 1700–1600 cm<sup>–1</sup> spectral region of the defatted BSA in D<sub>2</sub>O solution. Three-factor EFA has been employed to determine the distinction of the three protein species involved in the process of temperature elevation: native, transitional, and denatured protein. The temperature profiles obtained from three-factor EFA indicate that heat-induced conformational change in the secondary structures of defatted BSA in D<sub>2</sub>O undergoes two two-state transitions, a drastic transition and a slight transition, which occur in the temperature ranges of 68–82 °C and 56–76 °C, respectively.

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