Purification and characteristics of membrane-bound chitinase of anaerobic ruminal fungus Piromyces communis OTS1
| Autor: | Diego P. Morgavi, Yoshifumi Tomita, Kenji Komatani, Ryoji Onodera, Naomi Ushirone, Masaru Sakurada |
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| Přispěvatelé: | University of Miyazaki, Rowett Research Institute |
| Rok vydání: | 1998 |
| Předmět: |
Rumen
purification Size-exclusion chromatography Chitin Biology Applied Microbiology and Biotechnology Microbiology Cell wall Fungal Proteins 03 medical and health sciences affinity chromatography Affinity chromatography Extracellular Animals Anaerobiosis 030304 developmental biology chemistry.chemical_classification filtration 0303 health sciences 030306 microbiology Chromatofocusing Chitinases Fungi General Medicine Cytosol Enzyme [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology chemistry Biochemistry Chitinase biology.protein chromatography cell wall |
| Zdroj: | Current Microbiology Current Microbiology, Springer Verlag, 1998, 37 (1), pp.60-63. ⟨10.1007/s002849900338⟩ |
| ISSN: | 0343-8651 1432-0991 |
| DOI: | 10.1007/s002849900338⟩ |
| Popis: | International audience; A membrane-bound chitinase from cell wall fractions of the anaerobic ruminal fungus, Piromyces communis OTS1, was purified by affinity chromatography, gel filtration, and chromatofocusing. The molecular size of the chitinase was estimated by gel filtration to be 42.4 kDa and by SDS-PAGE to be 44.8 kDa, and its pI was 4.4. Activity was inhibited by Hg2+ and allosamidin. The activity at 39 degrees C was greatest at pH 6.0. It had an 'endo' type action. Solubilization tests indicated that plasmalemma-bound chitinase was held in place by an electrostatic type interaction. Characterization of the membrane-bound chitinase was more similar to that of extracellular chitinase than cytosolic chitinase. This suggested that membrane-bound chitinase was the origin of extracellular chitinase. |
| Databáze: | OpenAIRE |
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