期刊
CARBOHYDRATE RESEARCH
卷 343, 期 8, 页码 1316-1323出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.carres.2008.03.030
关键词
Serratia marcescens; chitosanase; chitosan; chitin; shrimp shell wastes
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. 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. (C) 2008 Elsevier Ltd. All rights reserved.
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