| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1388441 | Carbohydrate Research | 2008 | 4 Pages |
Abstract
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.
Graphical abstractThe 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.
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Authors
Songlin Li, Liang Chen, Chen Wang, Wenshui Xia,