Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050267 | FEBS Letters | 2009 | 6 Pages |
Abstract
Investigation of the xylanolytic enzyme system of the xylose-fermenting yeast Pichia stipitis resulted in the discovery of an extracellular α-glucuronidase efficiently debranching hardwood glucuronoxylan. This activity is not exhibited by more extensively investigated α-glucuronidases of glycoside hydrolase (GH) family 67, operating on substrates in which the uronic acid is linked to the non-reducing xylopyranosyl residues of main chain fragments. The N-terminus of the purified enzyme corresponded exactly to the P. stipitis gene ABN67901 coding for a protein of unknown function. BLAST search revealed the presence of similar genes in genomes of other microorganisms. These results lead to the emergence of a new family of α-glucuronidases.
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Authors
Olena Ryabova, Mária Vršanská, Satoshi Kaneko, Willem H. van Zyl, Peter Biely,