Multiple endoxylanases of Butyrivibrio sp.
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.
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Zootechnical Department, Biotechnical Faculty, University of Ljubljana, 1230 Domzale, Slovenia.
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D000818:Animals; D002417:Cattle; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D043364:Endo-1,4-beta Xylanases; D016965:Gram-Negative Anaerobic Straight, Curved, and Helical Rods / Q000201:enzymology* / Q000254:growth & development; D012417:Rumen / Q000382:microbiology; D014995:Xylosidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D003470:Culture Media; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases