Purification and characterization of an alpha-L-arabinofuranosidase from Butyrivibrio fibrisolvens GS113

Article Abstract:

An alpha-L-arabinofuranosidase, isolated and purified from the cytoplasm of Butyrivibrio fibrisolvens GS113 cells, was characterized to have a molecular mass of 240 kDa with an isoelectric point of 6.0. It is an octamer of a 31 kDa polypeptide and is active against substrates with an alpha-L-linkage and furanoside configuration. It is also capable of cleaving arabinose from varioussubstrates with alpha-linked arabinose side chains. Enzyme analysis suggests that this enzyme plays an important role in cell assimilation of arabinose-containing xylooligosaccharides.

Microbial enzymes

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Degradation and utilization of xylan by the ruminal bacteria Butyrivibrio fibrisolvens and Selenomonas ruminantium

Article Abstract:

The xylooligosaccharide-fermenting bacterium Selenomonas ruminantium and the xylanolytic bacterium Butyrivibrio fibrisolvens cross-feed on xylan hydrolysis products. The degradation of oat spelt xylan by B. fibrisolvens produces low-molecular weight xylooligosaccharides in the cultures. S. ruminantium grows on the products formed by extracellular xylanolytic enzymes of B. fibrisolvens on xylan. S. ruminantium degrades mono and disaccharides, lactate, glycerol and nucleic acids but has no action on polysaccharides.

Biodegradation, Xylem

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Degradation and utilization by Butyrivibrio fibrisolvens H17c of Xylans with different chemical and physical properties

Article Abstract:

Utilization of xylans by Butyrivibrio fibrisolvens appears to depend on the variability in xylan side chain type and distribution more than it depends on differences in the water solubility of xylans. Nine different xylans were assayed for degradation and utilization in B. fibrisolvens H17c, revealing differences between arabinoxylans and glucuronoxylans. Xylan utilization at 72 hours ranged from 57% to 92%.

Ruminants

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