new xylanase from a Trichoderma harzianum strain

A new xylanase (XYL2) was purified from solid-state cultures of Trichoderma harzianum strain C by ultrafiltration and gel filtration. SDS-PAGE of the xylanase showed an apparent homogeneity and molecular weight of 18 kDa. It had the highest activity at pH 5.0 and 45 degrees C and was stable at 50 de...

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Bibliographic Details
Published in:Journal of industrial microbiology & biotechnology 1999-07, Vol.23 (1), p.682-685
Main Authors: Silveira, F.Q. de P, Sousa, M.V. de, Ricart, C.A.O, Milagres, A.M.F, Medeiros, C.L. de, Filho, E.X.F
Format: Article
Language:English
Subjects:
Amino acids
Amino Acids - analysis
Biological and medical sciences
Biomass
Biotechnology
bleaching
Cellulase
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Enzyme engineering
Enzymes
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Miscellaneous
Molecular Weight
Plant biology
pretreatment
Proteins
pulp prebleaching
Sodium
Studies
Trichoderma - enzymology
Trichoderma harzianum
Ultrafiltration
Wood
wood pulp
Xylan Endo-1,3-beta-Xylosidase
Xylosidases - chemistry
Xylosidases - isolation & purification
Xylosidases - metabolism
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Summary:A new xylanase (XYL2) was purified from solid-state cultures of Trichoderma harzianum strain C by ultrafiltration and gel filtration. SDS-PAGE of the xylanase showed an apparent homogeneity and molecular weight of 18 kDa. It had the highest activity at pH 5.0 and 45 degrees C and was stable at 50 degrees C and pH 5.0 up to 4 h xylanase. XYL2 had a low K(m) with insoluble oat spelt xylan as substrate. Compared to the amino acid composition of xylanases from Trichoderma spp, xylanase XYL2 presented a high content of glutamate/glutamine, phenylalanine and cysteine, and a low content of serine. Xylanase XYL2 improved the delignification and selectivity of unbleached hardwood kraft pulp.
ISSN:1367-5435
1476-5535
DOI:10.1038/sj.jim.2900682