Purification and characterization of a xylanase from the thermophilic ascomyceteThielavia terrestris 255b |
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Authors: | Gilbert Michel Breuil Colette Yaguchi Makoto Saddler J. N. |
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Affiliation: | 1.Department of Biology, University of Ottawa, 30 Marie Curie, K1N 6N5, Ottawa, Ontario, Canada ;2.Chair of Forest Products Biotechnology, University of British Columbia, Forest Faculty, 270-2357 Main Mall, V6T 1W5, Vancouver, British Columbia, Canada ;3.Division of Biological Science, National Research Council of Canada, K1A 0R6, Ottawa, Ontario, Canada ; |
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Abstract: | Thielavia terrestris 255B, a thermophilic ascomycete, produced two major forms of xylanase with pIs of 4.6 (xylanase I) and 6.1 (xylanase II). The latter enzyme could be purified to > 99% homogeneity using anion-exchange chromatography and gel filtration. Xylanase II had a mol wt of 25.7 kDa (SDS-PAGE) and a pH and a temperature optimum of 3.6–4.0 and 60–65°C, respectively. The ratio of the enzyme’s activity against xylan and carboxymethylcellulose was 500–1000 to 1, indicating a possible application of this enzyme in biobleaching processes. The amino acid sequence of this protein is being determined, and initial data suggest that the enzyme belongs to a group of low-mol wt xylanases that have been isolated from both bacteria and fungi. |
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Keywords: | KeywordHeading" >Index Entries Thielavia terrestris xylanase thermophile |
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