Isolation and Chemical Composition of the Sheath ofSphaerotilus natans
| Autor: | Tomomi Nagase, Jun-ichi Koizumi, Minoru Takeda, Keishi Iohara, Fumio Nakano |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Surface Properties
medicine.medical_treatment Size-exclusion chromatography Glucuronates Polysaccharide Applied Microbiology and Biotechnology Biochemistry Dithiothreitol Analytical Chemistry chemistry.chemical_compound Glucuronic Acid medicine Amino Acids Sodium dodecyl sulfate Molecular Biology Fucose Gel electrophoresis chemistry.chemical_classification Chromatography Protease Gram-Negative Aerobic Bacteria integumentary system biology Sphaerotilus natans Polysaccharides Bacterial Organic Chemistry Galactose General Medicine biology.organism_classification Culture Media Glucose chemistry Lysozyme Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 62:1138-1143 |
| ISSN: | 1347-6947 0916-8451 |
| Popis: | A sheathed bacterium, Sphaerotilus natans, was cultured with vigorous shaking in a medium containing peptone. Then the biomass was harvested and treated with lysozyme, sodium dodecyl sulfate, and protease. With treatment, 1.6 mg of sheaths was obtained from 15 mg of biomass. For the preparation of sheaths of high purity, cultivation must be in the absence of glucose with sufficient aeration to prevent poly(3-hydroxybutyrate) accumulation. Carbohydrate (54.1%), protein (12.2%), and lipid (1-3%) were detected in the sheaths by colorimetric reactions and solvent extraction. Gas-liquid chromatography showed glucose and galactosamine to be present in the molar ratio of 1:4. The most abundant amino acids in the sheath protein were glycine (49.2 mol%) and cysteine (24.6 mol%). The sheaths were resistant to agents that reduce disulfide bonds (dithiothreitol and 2-mercaptoethanol) and to protease. However, sheathes were degraded completely by hydrazine, and a heteropolysaccharide composed of glucose and galactosamine (1:4) was released. The weight-average molecular weight of the polysaccharide was estimated to be 1.2 x 10(5) by gel filtration chromatography with a low-angle laser-light scattering photometer and a rotation index detector. A ladder of 1.5-kDa peptides separable by sodium dodecyl sulfate gel electrophoresis was obtained by partial hydrolysis of sheaths, suggesting the sheath protein has repeating units of 1.5 kDa. |
| Databáze: | OpenAIRE |
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