Effect of cyclodextrin on the activity and secondary structure of horseradish peroxidase

Protein Pept Lett. 2004 Dec;11(6):509-13. doi: 10.2174/0929866043406256.

Abstract

The activity and secondary structure of horseradish peroxidase (HRP) was studied in aqueous solution containing alpha-, beta- and gamma-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 alpha-helical structure was important for the activity of HRP. This phenomenon is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Circular Dichroism
  • Cyclodextrins / metabolism*
  • Horseradish Peroxidase / chemistry
  • Horseradish Peroxidase / metabolism
  • Peroxidases / chemistry
  • Peroxidases / metabolism*
  • Protein Structure, Secondary
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Cyclodextrins
  • Horseradish Peroxidase
  • Peroxidases