Deeper inside the specificity of lysozyme when degrading chitosan. A structural bioinformatics study.

ABSTRACT

Lysozymes that were used in numerous in vitro experiments of chitosan degradation were regularly from hen egg-white. Human lysozyme has been proved to be more active than hen egg-white lysozyme when exerting its bacteriostatic effect and there is possible that the two enzymes have some different structural properties. Consequently, within this study, we compared the structural and physicochemical properties of the human and egg-white lysozymes and used the molecular docking approach to obtain information concerning the specificity of the interactions between chitooligosaccharides with these enzymes. There is 60.47% of identity between the sequences of the human and the hen egg-white lysozymes, but the amino acids that are involved in the interactions of considered lysozymes with N-acetylchitohexaose are well conserved. Superimposition of the structures of investigated lysozymes reveals their structural similarity, the RMSD value being 1.198 Å for 118 equivalent carbon alpha atom pairs from a total of 129. There are some local physicochemical properties like the distribution of the electrostatic potential and the hydrophobicity of the catalytic cavities of the enzyme that are quite different. Substrate specificities of human and hen egg-white lysozyme with respect to chito-oligosaccharides are not clearly distinguishable but they are dependent on the molecular weight, deacetylation degree and pattern of deacetylation.