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. 1991 Jun;57(6):1860–1862. doi: 10.1128/aem.57.6.1860-1862.1991

Low-molecular-weight xylanase from Trichoderma viride.

M Ujiie 1, C Roy 1, M Yaguchi 1
PMCID: PMC183485  PMID: 1872616

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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