Denaturation and aggregation of lysozyme in water-ethanol solution.
We have applied rheological methods for the analysis of ethanol-lysozyme interaction during the process of denaturation and aggregation of the protein. At low concentration of ethanol a destruction of the hydration shell of lysozyme is observed. With the increase in the ethanol concentration a structural transformation takes place. It leads to the formation of a protein aggregate with an elongated structure. The rheological characteristics of lysozyme-water-ethanol solution changes from Newtonian to pseudoplastic.
Faculty of Physics, Department of Molecular Biophysics, Adam Mickiewicz University, Poznań, Poland.
Agnieszka
A
Szymańska
Tomasz
T
Hornowski
Genowefa
G
Ślósarek
D000818:Animals; D002642:Chick Embryo; D000431:Ethanol / Q000737:chemistry*; D008027:Light; D009113:Muramidase / Q000737:chemistry*; D011489:Protein Denaturation; D020836:Protein Structure, Quaternary; D012212:Rheology; D012542:Scattering, Radiation; D033081:Shear Strength; D012997:Solvents / Q000737:chemistry*; D014783:Viscosity; D014867:Water / Q000737:chemistry*
D012997:Solvents; D014867:Water; D000431:Ethanol; D009113:Muramidase