Purification and Characterization of Lysozyme From the Egg Of Japanese Quail Coturnix coturnix japonica

Abstract

The present study, the quail egg lysozyme was extracted, purified and characterized for its secondary structure. The protein’s concentration was estimated by colourimetrically using BSA as a standard. Chromatography was performed with G-100 column to get the purest form of the enzyme. The extent of purity was confirmed by running native PAGE. The molecular weight of purified lysozyme was also determined by SDS-PAGE. Similarly, the sample was used for its secondary structure conformational studies using infra red (IR), the spectrum gave a peak at 1643.2 cm^-1 showing the existence of a helix. Also the same was further confirmed by standard plot. The conformational investigations have been carried out on lysozyme, in which measurements of the reduced molar ellipticitiesshowed the presence of lysozyme, and observed negative circular dichroism (CD) band at 207 nm and a shoulderaround 221 nm. Results were in agreement with standard ellipticity data. The conformationalchanges revealed by CD data measurements showed alpha helix conformations. All these studies were carried only after the protein was purified from quail egg white.