Author/Editor		Marinšek-Logar, Romana; Gasparič, A; Nekrep, FV
Title		Ksilanolitični encimski kompleks vampne bakterije Prevotella bryantii B1 4
Translated title		Xylanolytic enzyme complex of rumen bacterium Prevotella bryantii B1 4
Type		članek
Source		In: Bole-Hribovšek V, Ocepek M, Klun N, editors. Zbornik s programom 2. kongres slovenskih mikrobiologov z mednarodno udeležbo; 1998 sep 27-30; Portorož. Ljubljana: Slovensko mikrobiološko društvo,
Publication year		1998
Volume		str. 300-3
Language		slo
Abstract		Prevotella spp. are recognised as one of the most numerous strictly anaerobic bacteria inhabiting the rumen. Potentially significant activities include the degradation of plant cell wall polyaccharides, starch, proteins and peptides. P. bryantii B14 is not cellulolytic but actively degrades hemicellulose xylan and carries multiple xylanase genes. Four regions encoding xylanase activity have been isolated, one of which corresponds to a broad - specifity endoglucanase. Of the remaining regions, one encodes activities against p-nitrophenyl-beta-xyloside and p-nitrophenyl-alfa-L-arabinofuranoside (genes zyn A and xynB). The gene xynC encodes another endoxylanase. SDS PAGE xylanograms revealed four endoxylanolytic bands at 29 kDa, kDa, 66 kDa and 88 kDa. Following a cell fractionation procedure the majority of endoxylanase and CMC-ase activity was found in periplasmic cell fraction while most of the alpha-L-arabinofuranosidase and beta-xylosidase activities were found in the crude membrane fraction. HLPC separation of periplasmic proteins by BIA CIM DEAE tubes resulted in partial isolation of CMC-ase and 66-kDa endoxylanase. These enzymes probably act sequentially and synergistically with the enzymes of other xylanolytic and cellulolytic microorganisms in the degradation of xylan in vivo.
Descriptors		PREVOTELLA XYLANS ARABINOFURANOSYLURACIL XYLOSIDASES