Thermal Stability of Hen egg white lysozyme (HEWL) with Ni(II)salen

Schiff bases drived from Salicylaldehyde and diamines as N,N'-bis (Salicylaldehyd) ethylene diamine are one of the most synthetic ligand system with important in asymmetric catalysis[۱]. In the area of bioinorganic chemistry interest in Schiff-base complex has containing sites in metallo-proteins and metallo enzymes [۲]. Lysozyme is a global protein, cosists of ۱۲۹ amino acids with a molecular weight of about ۱۴.۳KD. Its structure is stabilized by four disulfide bridges and the interior of the protein is almost hydrophobic while the surface is mostly polar[۳,۴].So,In the present work thermal denaturation of lysozyme has been studied and the melting point of lysozyme in the presences and absences of Ni(II)Salen [Salen :N,N'-bis(Salicydene)۱,۲-diamino ethane] to analysis denaturation data we use Sigma plot and Igor softwores

کلیدواژه ها:

Lysozyme ، Ni(II)Salen ، Thermal stability ، Denaturation and Schiff base.