화학공학소재연구정보센터
Applied Microbiology and Biotechnology, Vol.47, No.3, 231-235, 1997
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 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 beta-nitrophenyl alpha-L-arabinofuranoside or towards sugar-beet arabinan, soy arabinogalactan, arabino-oligosaccharides and arabinogalacto-oligosaccharides.