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Low-molecular-weight xylanase from Trichoderma viride.

M Ujiie·C Roy·M Yaguchi
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Abstract

An endo-1,4-beta-xylanase (1,4-beta-D-xylan xylanohydrolase, EC 3.2.1.8) 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.

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Amino Acid SequenceAmino AcidsElectrophoresis, Polyacrylamide GelEndo-1,4-beta XylanasesGlycoside HydrolasesMolecular Sequence DataMolecular WeightSequence Homology, Nucleic AcidTrichodermaJournal Article

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M Ujiie, C Roy, M Yaguchi. 1991. Low-molecular-weight xylanase from Trichoderma viride.. https://doi.org/10.1128/aem.57.6.1860-1862.1991

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