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°C and was stable at 50°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.
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Received 02 February 1999/ Accepted in revised form 17 April 1999
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de Paula Silveira, F., de Sousa, M., Ricart, C. et al. A new xylanase from a Trichoderma harzianum strain. J Ind Microbiol Biotech 23, 682–685 (1999). https://doi.org/10.1038/sj.jim.2900682
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DOI: https://doi.org/10.1038/sj.jim.2900682