Abstract
The activity and secondary structure of horseradish peroxidase (HRP) was studied in aqueous solution containing α-, β- and γ-cyclodextrin (CD). The results showed that the activity of HRP was enhanced to different extents by the three kinds of CD. A Fourier Transform infrared (FTIR) spectroscopy study indicated that the amount of α-helical structure was important for the activity of HRP. This phenomenon is discussed.
Keywords: horseradish peroxidase, cyclodextrin, fourier transform infrared, secondary structure, helical, sheet