Purification and mode of action of two different arabinoxylan arabinofuranohydrolases from Bifidobacterium adolescentis DSM 20083 |
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Authors: | K M J Van Laere C H L Voragen T Kroef L A M Van den Broek G Beldman A G J Voragen |
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Institution: | (1) Department of Food Technology and Nutritional Sciences, Food Science Group, Wageningen Agricultural University, PO Box 8129, 6700 EV Wageningen, The Netherlands Tel.: +31-317-481888 Fax: +31-317-484893, NL |
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Abstract: | Two novel arabinofuranohydrolases (AXH-d3 and AXH-m23) were purified from Bifidobacterium adolescentis DSM 20083. Both enzymes were induced upon growth of Bi. adolescentis on xylose and arabinoxylan-derived oligosaccharides. They were only active with arabinoxylans and therefore denoted as arabinoxylan
arabinofuranohydrolases. Their optimal activity was at pH 6 and 30–40 °C. They were very specific in their mode of action
and were clearly different from AXH-m from Aspergillus awamori. AXH-m23 released only arabinosyl groups, which were linked to the C-2 or C-3 position of singly substituted xylose residues
in arabinoxylan oligomers. AXH-d3 hydrolysed C-3-linked arabinofuranosyl residues of doubly substituted xylopyranosyl residues
of arabinoxylans and arab- inoxylan-derived oligosaccharides. No activity was observed with C-2-linked arabinofuranosyl residues
of these doubly substituted xylopyranosyl residues, or against C-2- and C-3-linked arabinofuranosyl residues of singly substituted
xylopyranosyl residues. The combination of AXH-d3 and AXH-m showed low debranching activity with highly substituted glucurono-arabinoxylans.
However, arabinoxylan from wheat flour was debranched almost completely.
Received: 12 January 1999 / Accepted: 17 January 1999 |
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