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. 2001;46(1):94-6.
doi: 10.1007/BF02825897.

Multiple endoxylanases of Butyrivibrio sp

M Zorec  1 , T Cepeljnik, F V Nekrep, R M Logar
Affiliations

Multiple endoxylanases of Butyrivibrio sp

M Zorec et al. Folia Microbiol (Praha). 2001.

Abstract

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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