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Partition and purification of lysozyme from quail egg white using aqueous two phase system

Senthilkumar Rathnasamy, B.N.Vedhahari, R.Kumaresan

Lysozyme, one of themost expensive and commercially available enzymes is mostly exploited fromthe chicken egg white. It is commercially used as a cell disrupting agent, food additive and in the treatment of ulcers and infections. It is an antimicrobial enzyme that hydrolyzes the beta-glycosidic linkage between N-acetylmuramic acid and N-acetyl glucosamine in the peptidoglycan of bacterial cell walls and can also bind to polymers of Nacetyl glucosamine. This study focuses on the isolation and purification of the enzyme from Quail egg white. Experiments were carried out using Ammoniumsulphate precipitation andAqueous two phase extraction and the protein content was found to be high inAqueous two phase extraction when compared to the Ammonium sulphate precipitation. The protein concentration and enzyme activity were estimated using LowryÂ’s method and turbidimetric assay respectively. The purification process was further increased by performing Gel filtration Chromatography and the fractions were confirmed using 12%SDS gel and the molecular weightwas found to be ~14kDawhich is almost similar to that of the chicken egg. The secondary structure of lysozyme extracted from Quail egg white was performed by FTIR analysis and compared against standard lysozyme sample.