Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1386230 | Carbohydrate Research | 2005 | 8 Pages |
Abstract
An oligoxyloglucan reducing end-specific xyloglucanobiohydrolase from the filamentous fungus Aspergillus nidulans was cloned and expressed in Pichia pastoris as a secreted histidine-tagged protein and purified by affinity chromatography. The enzyme acts on xyloglucan oligomers and releases the first two glycosyl residue segments from the reducing end, provided that neither the first glucose nor the xylose attached to the third glucose residue from the reducing end is not further substituted. The enzyme has a specific activity of 7 U/mg at the pH optimum of 3 and at the temperature optimum of 42 °C.
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Related Topics
Physical Sciences and Engineering
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Organic Chemistry
Authors
Stefan Bauer, Prasanna Vasu, Andrew J. Mort, Chris R. Somerville,