Low-molecular-weight xylanase from Trichoderma viride

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Journal titleApplied and Environmental Microbiology
Pages18601862; # of pages: 3
AbstractAn endo-1,4-beta-xylanase (1,4-beta-D-xylan xylanohydrolase, EC has been isolated from a commercial preparation of Trichoderma viride. The molecular weight was 22,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the pI value was 9.3. The xylanase was a true xylanase without cellulase activity. When the N-terminal amino acid sequence of the first 50 residues was compared with that of a xylanase from Schizophyllum commune, strong evidence for homology was found, with more than 50% amino acid identity. T. viride xylanase also possessed extensive identity with a proposed amino-terminal consensus sequence of xylanases from bacteria.
Publication date
AffiliationNational Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedNo
NRC numberUJIIE1991
NPARC number9384922
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Record identifier999a5850-02df-4578-b2a7-6d97ca0844af
Record created2009-07-10
Record modified2016-05-09
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