A NEW ARABINOFURANOHYDROLASE FROM BIFIDOBACTERIUM-ADOLESCENTIS ABLE TO REMOVE ARABINOSYL RESIDUES FROM DOUBLE-SUBSTITUTED XYLOSE UNITS IN ARABINOXYLAN

An arabinofuranohydrolase (AXH-d3) was from a cell-free extract of Bif idobacterium adolescentis DSM 20083. The enzyme had a molecular mass o f approximately 100 kDa as determined by gel filtration. It displayed maximum activity at pH 6 and 30 degrees C. Using an arabinoxylan-deriv ed oligosaccharide containing double-substituted xylopyranosyl residue s established that the enzyme specifically released terminal arabinofu ranosyl residues linked to C-3 of double-substituted xylopyranosyl res idues. In addition, this arabinofuranohydrolase released arabinosyl gr oups from wheat flour arabinoxylan polymer but showed no activity towa rds beta-nitrophenyl alpha-L-arabinofuranoside or towards sugar-beet a rabinan, soy arabinogalactan, arabino-oligosaccharides and arabinogala cto-oligosaccharides.