An alpha-L-arabinofuranosidase produced by the fungus Aspergillus awamori had a molecular mass of approximately 64 kDa on sodium dodecyl sulphate/polyacrylamide gel electrophoresis (SDS-PAGE) and was optimally active at pH 4.6 and 50 degrees C. The enzyme, which chromatographed as a single component on SDS-PAGE, appeared to consist of two isoenzymes of pI 3.6 and 3.2. Acting in isolation, the alpha-L-arabinofuranosidase had only a very limited capacity to release L-arabinose (less than 11%) directly from arabinoxylans that had been extracted from a number of plant cell wall preparations using 18% alkali, but a much higher proportion of the L-arabinose (46%) was released from a wheat straw arabinoxylan that had been isolated by steam treatment. There was a marked synergistic effect between the alpha-L-arabinofuranosidase and an endo-(1 --> 4)-beta-D-xylanase produced by A. awamori in both the rate and extent of the release of L-arabinose from both oat straw and wheat straw arabinoxylans, suggesting that L-arabinose-substituted oligosaccharides generated by the endoxylanase action were better substrates for enzyme action. A novel property of the alpha-L-arabinofuranosidase was its capacity to release a substantial proportion (42%) of feruloyl L-arabinose from intact wheat straw arabinoxylan. The concerted action of the alpha-L-arabinofuranosidase and endoxylanase released 71% of the feruloyl L-arabinose and 69% of the p-coumaroyl L-arabinose substituents from the wheat straw arabinoxylan.