Circular dichroism and fluorescence spectroscopy studies of the effect of cyclodextrins on the thermal stability of chicken egg white lysozyme in aqueous solution
Tatsuyuki Yamamoto, Noriko Fukui, Akihiro Hori, Yoshihisa Matsui
Journal of Molecular Structure
Circular dichroism spectroscopy revealed that the thermal stability of chicken egg white lysozyme in an aqueous buffer solution is significantly lowered by the addition of 6-O-α-d-glucosyl-β-cyclodextrin (G1-β-CD), whereas it is raised by the addition of methyl α-d-glucopyranoside. The α- and γ-cyclodextrin also lowered the thermal stability, although the effects were less prominent than that of G1-β-CD. Fluorescence spectroscopy suggested that cyclodextrins include the side chains of tryptophan residues within their internal cavities to lower the thermal stability of lysozyme. The fluorescence intensity of a sample, re-cooled to 25 °C after thermal denaturation at 75 °C in the presence of G1-β-CD, was stronger than that observed for native lysozyme. The fact that the fluorescence intensity of the re-cooling sample was stronger than that of the native one indicates that G1-β-CD persists in binding to the side chains of tryptophan residues of the re-cooled lysozyme.
Circular dichroism, Protein folding, Thermal stability, Protein denaturation, Secondary structure, Biochemistry