Van Laere K M, Beldman G, Voragen A G
Department of Food Science, Wageningen Agricultural University, The Netherlands.
Appl Microbiol Biotechnol. 1997 Mar;47(3):231-5. doi: 10.1007/s002530050918.
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.
从青春双歧杆菌DSM 20083的无细胞提取物中纯化出一种阿拉伯呋喃水解酶（AXH-d3）。通过凝胶过滤测定，该酶的分子量约为100 kDa。它在pH 6和30℃时表现出最大活性。使用含有双取代木吡喃糖基残基的阿拉伯木聚糖衍生寡糖确定，该酶特异性地释放与双取代木吡喃糖基残基的C-3相连的末端阿拉伯呋喃糖基残基。此外，这种阿拉伯呋喃水解酶能从小麦粉阿拉伯木聚糖聚合物中释放阿拉伯糖基，但对对硝基苯基α-1-阿拉伯呋喃糖苷、甜菜阿拉伯聚糖、大豆阿拉伯半乳聚糖、阿拉伯寡糖和阿拉伯半乳寡糖没有活性。
