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- Title
Purification and characterization of chitinases from Clostridium sp. E-16 isolated from the intestinal tract of the South American sea lion ( Otaria flavescens).
- Authors
Konagaya, Y.; Tsuchiya, C.; Sugita, H.
- Abstract
Aims: This study was undertaken to examine the properties of chitinases purified from Clostridium sp. E-16, an intestinal bacterium of the South American sea lion ( Otaria flavescens). We also elucidated the taxonomic status of this bacterium to better understand the role of intestinal anaerobic bacteria in marine animals. Methods and Results: Two chitinases were purified with ammonium sulfate precipitation, affinity chromatography and preparative electrophoresis from culture supernatant fluid from Clostridium sp. E-16. Molecular mass was estimated to be 77 kDa for chitinase 1 and 98 kDa for chitinase 2 by SDS-PAGE. Optimum pH of both purified chitinases was between 5·0 and 7·0. Chitinase 1 was inhibited with Cu2+, Fe2+, Hg2+ and Zn2+, while chitinase 2 was inhibited with Fe2+. Phylogenetic analysis using 16S ribosomal DNA (rDNA) sequences and phenotypic characterization revealed that Clostridium sp. E-16 was closely related to Clostridium baratii. Conclusions: It is likely that chitinases from C. baratii or a C. baratii-like bacterium play an important role in degradation of chitin in the intestinal tract of the South American sea lion and in marine environments. Significance and Impact of the Study: This is the first report of chitinase purification and characterization from a marine Clostridium strain.
- Subjects
SOUTH America; CHITINASE; CLOSTRIDIUM; SEA lions; AFFINITY chromatography; BACTERIAL physiology
- Publication
Letters in Applied Microbiology, 2006, Vol 43, Issue 2, p187
- ISSN
0266-8254
- Publication type
Article
- DOI
10.1111/j.1472-765X.2006.01926.x