TY - JOUR
T1 - Purification and characterization of a chitosanase from Serratia marcescens TKU011
AU - Wang, San Lang
AU - Peng, Jo Hua
AU - Liang, Tzu Wen
AU - Liu, Kao Cheng
N1 - Funding Information:
This work was supported in part by a grant of the National Science Council, Taiwan (NSC95-2313-B-032-003).
PY - 2008/6/9
Y1 - 2008/6/9
N2 - 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 °C, pH 4-8, and <50 °C, respectively. The chitosanase was inhibited completely by EDTA, Mn2+, and Fe2+. 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.
AB - 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 °C, pH 4-8, and <50 °C, respectively. The chitosanase was inhibited completely by EDTA, Mn2+, and Fe2+. 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.
UR - https://www.scopus.com/pages/publications/43049117464
UR - https://www.scopus.com/pages/publications/43049117464#tab=citedBy
U2 - 10.1016/j.carres.2008.03.030
DO - 10.1016/j.carres.2008.03.030
M3 - Article
C2 - 18420186
AN - SCOPUS:43049117464
SN - 0008-6215
VL - 343
SP - 1316
EP - 1323
JO - Carbohydrate Research
JF - Carbohydrate Research
IS - 8
ER -