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Showing content from https://link.springer.com/doi/10.1007/s002530050918 below:

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 °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 α-l-arabinofuranoside or towards sugar-beet arabinan, soy arabinogalactan, arabino-oligosaccharides and arabinogalacto-oligosaccharides.

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1. Section Food Chemistry and Microbiology, Department of Food Science, Wageningen Agricultural University, PO Box 8129, 6700 EV Wageningen, The Netherlands. Fax +31 317 484893, , , , , , NL

   K. M. J. Van Laere, G. Beldman & A. G. J. Voragen

1. K. M. J. Van Laere
2. G. Beldman
3. A. G. J. Voragen

Received: 15 July 1996 / Received revision: 18 October 1996 / Accepted: 18 October 1996

Laere, K., Beldman, G. & Voragen, A. A new arabinofuranohydrolase from Bifidobacterium adolescentis able to remove arabinosyl residues from double-substituted xylose units in arabinoxylan. Appl Microbiol Biotechnol 47, 231–235 (1997). https://doi.org/10.1007/s002530050918

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• Issue Date: March 1997

• DOI: https://doi.org/10.1007/s002530050918

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