Abstract
A chitosanase from the snail of Achatina fulica was purified 18.27-fold with 0.68% recovery of protein and 12.53% recovery of enzymatic activity by phenyl-sepharose column chromatography, diethylaminoethanol (DEAE)-sepharose column chromatography and Sephacryl S-300 gel filtration. The molecular mass of chitosanase was 72 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the isoelectric point (pI) of purified chitosanase was 5.45 estimated by isoeletrofocusing electrophoresis. The Km measured for the chitosanase was 0.154 μM, with an apparent V max of 0.005 μM/min. The current work for the first time obtains a chitosanase from A. fulica might be potentially served as a useful enzyme for hydrolyzing chitosan. It is purified as an important initial material for mass spectrometric sequencing, gene cloning and protein expression of this chitosanase. Keywords: Achatina fulica , chitosanase, purification, characterization
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