spectroscopic studies of the interaction of lysozyme and zno nanoparticles

abstract adsorption of proteins on inorganic surfaces may lead to structural and functional changes that are dependent on both the nature of the adsorbed proteins and the physicochemical properties of the inorganic surfaces. chicken egg white lysozyme (e.c 3.2.1.17, mw=14.6 kda) is a small globular protein, that consists of 129 amino acid residues with four disulfide bonds. the aim of this study was the survey of the stability and structure of chicken egg white lysozyme against zno nano through thermal stability, fluorescence and spectroscopy and enzyme activity assay in the absence or presence of zno nano particle at ph 7.0. the obtained results indicated that thermal stability and activity of lysozyme decreased with increase in zno nanoparticles concentration. moreover, it was observed that zno nano particle quenched the intrinsic fluorescence of lysozyme. the interaction studies of zno nanoparticles and lysozyme show that not only water and solvent molecules can effect on 3d structure of lysozyme and protein but also play an important role in adsorption nanoparticles.