Expression, purification and characterization of endo-type chitosanase of Aspergillus sp. CJ22-326 from Escherichia coli

An endo-chitosanase gene was cloned from Aspergillus sp. CJ22-326 and expressed in Escherichia coli. The purified protein showed an endo-chitosanase activity during viscosimetric assay and TLC analysis. The enzyme had higher chitosanolytic activity than previously reported fungal chitosanases.

The cDNA encoding endo-chitosanase from Aspergillus sp. CJ22-326 was cloned, expressed and its product was purified from E.coli. Chitosanase activity of the recombinant protein was much higher than other heterologous expression fungal proteins.