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  • Title: Purification and characterization of a chitosanase from Serratia marcescens TKU011.
    Author: Wang SL, Peng JH, Liang TW, Liu KC.
    Journal: Carbohydr Res; 2008 Jun 09; 343(8):1316-23. PubMed ID: 18420186.
    Abstract:
    A chitosanase was purified from the culture supernatant of Serratia marcescens TKU011 with shrimp shell wastes as the sole carbon/nitrogen source. Zymogram analysis revealed the presence of chitosanolytic activity corresponding to one protein, which was purified by a combination of ion-exchange and gel-filtration chromatography. The molecular weight of the chitosanase was 21 kDa and 18 kDa estimated by SDS-PAGE and gel-filtration, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of the chitosanase were 5, 50 degrees C, pH 4-8, and <50 degrees C, respectively. The chitosanase was inhibited completely by EDTA, Mn(2+), and Fe(2+). The results of peptide mass mapping showed that three tryptic peptides of the chitosanase were identical to a chitin-binding protein Cbp21 from S. marcescens (GenBank accession number gi58177632) with 63% sequence coverage.
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