Isolation and purification of lysozyme from albumin: Effect of albumin concentration, pH and ionic strength of buffer solution [Pemisahan dan penulenan lisozim dari albumin: Kesan kepekatan albumin, pH dan kekuatan ionik larutan penimbal]

Abstract

The low content of lysozyme in albumin makes its purification process becomes complicated and challenge either in lab or industrial scale system. This study aimed to investigate the parameters influencing the purification performance lysozyme from chicken egg white (CEW) namely initial concentration of albumin, pH and ionic strength of buffer solution. Immobilized metal affinity chromatography (IMAC) beads were prepared using chitosan-coated silica beads which then crosslinked with glutaraldehyde (GTA) and reacted with metal ion copper (Cu) for metal ion immobilization to be used as purificati on tool s. The prepared beads were characterized in term of morphology and structure using scanning electron microscope (SEM). Column chromatographic has been utilized for evaluation performance of IMAC for lysozyme separation. Optimum recovery obtained usi ng 20 mg/ml CEW concentration at pH 7, with 0.05 M ionic strength. The finding of this study exhibited a good pathway to design an affinity system for lysozyme purification either from chicken egg white or other sources in the future