Purification and characterization of a xylanase from the thermophilic ascomycete Thielavia terrestris 255B

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DOIResolve DOI: http://doi.org/10.1007/BF02920549
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TypeArticle
Journal titleApplied Biochemistry and Biotechnology
Volume34-35
Issue1
Pages247259; # of pages: 13
AbstractThielavia 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.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedNo
NRC numberGILBERT1992
NPARC number9380275
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Record identifier35f246a4-4ca8-4cca-abca-bb146f855879
Record created2009-07-10
Record modified2016-05-09
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