Multiple endoxylanases of Butyrivibrio sp
| Autor: | T. Čepeljnik, Maša Zorec, R. Marinšek Logar, F. V. Nekrep |
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| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
animal structures Endo-1 4-beta Xylanases Rumen biology Size-exclusion chromatography Ion chromatography General Medicine biology.organism_classification Microbiology Xylan Enzyme assay Culture Media Gram-Negative Anaerobic Straight Curved and Helical Rods Enzyme Xylosidases chemistry Biochemistry Butyrivibrio biology.protein Animals Zymography Cattle Electrophoresis Polyacrylamide Gel Bacteria |
| Zdroj: | Folia microbiologica. 46(1) |
| ISSN: | 0015-5632 |
| Popis: | Butyrivibrio sp. Mz 5 with a high xylanolytic activity was isolated. Four major xylanases were detected in the cell-associated fraction using the zymogram technique. The xylanolytic activity was inducible with the oat spelts xylan; two endoxylanases (51 and 145 kDa) were formed constitutively. The bulk of the xylanolytic activity was cell-bound and growth-phase dependent; the maximum activity in the cell-associated fraction was achieved after 16 h of incubation. The highest xylanolytic activity was determined in a medium with 0.5% oat spelts xylan. Under optimum conditions (the highest xylanolytic activity produced), the two cell-bound xylanases (51 and 58 kDa) were isolated by anion exchange chromatography on CIM DEAE 8 tubes attached to a MPLC system, and gel filtration. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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