journal article Jul 30, 2014

Trichoderma reesei XYN VI – a novel appendage‐dependent eukaryotic glucuronoxylan hydrolase

The FEBS Journal Vol. 281 No. 17 pp. 3894-3903 · Wiley
View at Publisher Save 10.1111/febs.12925
Abstract
Expression of a Trichoderma reesei gene coding for a putative GH30 xylanase in Aspergillus oryzae led to isolation and purification of a novel xylanase exhibiting catalytic properties different from those of the previously characterized GH30 xylanase XYN IV of T. reesei. The novel enzyme, named XYN VI, exhibited catalytic properties similar to appendage‐dependent GH30 glucuronoxylanases previously recognized only in bacteria. XYN VI showed high specific activity only on xylans or xylooligosaccharides containing 4‐O‐methyl‐d‐glucuronic acid or d‐glucuronic acid side substituents. The cleavage of the main chain takes place primarily at the second glycosidic linkage from the branch towards the reducing end of the polysaccharides or aldouronic acids. These catalytic properties resemble bacterial GH30 glucuronoxylanases, although the recognition of the uronic acid side chains by XYN VI is apparently based on interaction of the substrate with other amino acids. Moreover, in contrast to bacterial enzymes, XYN VI is also capable of slower but significant cleavage of unsubstituted parts of xylan and acidic xylooligosaccharides. The data point to a great catalytic diversity of xylanases produced by the most extensively studied cellulolytic fungus.
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Metrics
51
Citations
34
References
Details
Published
Jul 30, 2014
Vol/Issue
281(17)
Pages
3894-3903
License
View
Funding
Slovak Research and Development Agency Award: APVV 0602 12
Cite This Article
Peter Biely, Vladimír Puchart, Mary Ann Stringer, et al. (2014). Trichoderma reesei XYN VI – a novel appendage‐dependent eukaryotic glucuronoxylan hydrolase. The FEBS Journal, 281(17), 3894-3903. https://doi.org/10.1111/febs.12925
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