Abstract
We investigate the thermal denaturation of solid bovine serum albumin (BSA) using terahertz time domain spectroscopy (THz-TDS). When the protein is heated up from 25°C to 107°C and cooled down to 25°C again, an irreversible decrease in its THz absorption coefficient and refractive index is observed. The corresponding frequency-dependent permittivity during heating is fitted by the Debye model with single relaxation time. The relaxation times during temperature rising agree very well with Arrhenius equation with the activation energy of 6.52kJ/(K·mol), which can be an indicator for the stability of BSA during thermal denaturation process.
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