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Purification and characterization of a (1,4)-β-d-arabinoxylan arabinofuranohydrolase from Aspergillus awamori

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Summary

An enzyme able to split off arabinose sidechains from cereal arabinoxylans was isolated from a cell-free culture filtrate of Aspergillus awamori CMI 142717 containing milled oat straw as the carbon source. The enzyme was highly specific for arabinoxylans and, unlike other α-l-arabinofuranosidases reported in the literature, did not show any activity towards p-nitrophenyl α-l-arabinofuranoside, arabinans and arabinogalactans. This novel enzyme, which can be described as a (1,4)-β-d-arabinofuranohydrolase, had a molecular mass of 32 000 Da when determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and a specific activity of 22 units/mg on wheat arabinoxylan.

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Kormelink, F.J.M., Searl-Van Leeuwen, M.J.F., Wood, T.M. et al. Purification and characterization of a (1,4)-β-d-arabinoxylan arabinofuranohydrolase from Aspergillus awamori . Appl Microbiol Biotechnol 35, 753–758 (1991). https://doi.org/10.1007/BF00169890

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  • DOI: https://doi.org/10.1007/BF00169890

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