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.

Zootechnical Department Biotechnical Faculty University of Ljubljana 1230 Domzale Slovenia

Zobrazit více v PubMed

Appl Environ Microbiol. 1991 Jul;57(7):2016-20 PubMed

Nature. 1970 Aug 15;227(5259):680-5 PubMed

Biotechniques. 2000 Mar;28(3):426-8, 430, 432 PubMed

Anal Biochem. 1977 Jul;81(1):21-7 PubMed

FEMS Microbiol Lett. 1991 Nov 15;68(2):197-203 PubMed

Microbiol Rev. 1988 Sep;52(3):305-17 PubMed

Appl Environ Microbiol. 1987 Dec;53(12):2849-53 PubMed

J Chromatogr A. 1997 Jan 24;760(1):117-23 PubMed

Identification of GH10 xylanases in strains 2 and Mz5 of Pseudobutyrivibrio xylanivorans

Isolation of Pseudobutyrivibrio ruminis and Pseudobutyrivibrio xylanivorans from rumen of Creole goats fed native forage diet

Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorans Mz5T

Purification and characterization of xylanases from Aspergillus giganteus

Is Pseudobutyrivibrio xylanivorans strain Mz5T suitable as a probiotic? An in vitro study