A new arabinofuranohydrolase from Bifidobacterium adolescentis able to remove arabinosyl residues from double-substituted xylose units in arabinoxylan.
An arabinofuranohydrolase (AXH-d3) was purified from a cell-free extract of Bifidobacterium adolescentis DSM 20083. The enzyme had a molecular mass of approximately 100 kDa as determined by gel filtration. It displayed maximum activity at pH 6 and 30 degrees C. Using an arabinoxylan-derived oligosaccharide containing double-substituted xylopyranosyl residues established that the enzyme specifically released terminal arabinofuranosyl residues linked to C-3 of double-substituted xylopyranosyl residues. In addition, this arabinofuranohydrolase released arabinosyl groups from wheat flour arabinoxylan polymer but showed no activity towards p-nitrophenyl alpha-1-arabinofuranoside or towards sugar-beet arabinan, soy arabinogalactan, arabino-oligosaccharides and arabinogalacto-oligosaccharides.
Van Laere
K M
KM
Department of Food Science, Wageningen Agricultural University, The Netherlands.
Beldman
G
G
Voragen
A G
AG
D001644:Bifidobacterium / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D014990:Xylans / Q000378:metabolism*; D014994:Xylose / Q000378:metabolism*
D014990:Xylans; C085118:arabinoxylan; D014994:Xylose; D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase