کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1388686 | 982810 | 2008 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Purification and characterization of a chitosanase from Serratia marcescens TKU011 Purification and characterization of a chitosanase from Serratia marcescens TKU011](/preview/png/1388686.png)
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.
Time courses of chitosanase production in a culture of Serratia marcescens TKU011 on shrimp shell containing media: (
• ) protease activity (U/mL); (▴) chitosanase activity (U/mL); (∘) pH; (■) OD660.Figure optionsDownload as PowerPoint slide
Journal: Carbohydrate Research - Volume 343, Issue 8, 9 June 2008, Pages 1316–1323