Purification and properties of lysozyme from a marine strain

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An extracellular lysozyme from a new strain which was screened from a sea mud sample was purified to homogeneity by ultrafiltration, followed by ammonium sulphate precipitation, dialysis, Sephadex G-100 chromatography and CM-Sephadex-50 ionexchange chromatography. This purification protocol resulted in a 65.28 fold purification of lysozyme with 17.68% final yield and the relative molecular weight of the enzyme was determined to be 16.0 kDa by SDS-PAGE. The kinetic characterisation of the purified enzyme exhibited maximum activity at 35°C and pH 8.0. The enzyme activity was promoted in the presence of Zn 2+ and Cu 2+ , and inhibited by Mn 2+ . EDTA did not affect the enzyme activity. The enzyme was highly stable in the presence of several thickening agents. Some surfactants increased its activity. It had a broad antimicrobial spectrum against several Gram positive bacteria, Gram negative bacteria and fungi. The enzyme has broad potential application.