Differences in bleaching responses from fungal- versus bacterial-derived enzymes

Several mills in North America have been successful in using xylanase enzymes expressed from Trichoderma reesei (a fungus) as part of their bleaching sequence for many years. These mills process hardwood and softwood species, with and without oxygen delignification. These mills also use three-, four-, and five-stage bleaching sequences. North American mills tend to report increased pulp brightness ceilings and decreased bleaching costs as benefits associated with the application of enzymes in the bleaching process. Laboratory testing suggests that eucalyptus pulp is highly susceptible to fungal- and bacterial-derived enzyme bleaching and should result in significant cost savings in South American mills. At least four different mills in South America have attempted to perform enzyme bleaching trials using bacterial-derived enzymes. Each of these mill trials resulted in significantly increased operating costs and/or unsustainable operating conditions. More recently, one of these South American mills performed a short trial using a commercially available, fungal-derived enzyme. This trial was technically successful. This report attempts to determine why the South American mill experiences with bacterial-derived enzymes have been poor, while North American mills and the one South American mill trial have had good results with fungal-derived enzymes. Operating conditions and trial goals for the North and South American mills also were examined.

Fate of Residual Lignin during Delignification of Kraft Pulp by Trametes versicolor

ABSTRACT The fungus Trametes versicolor can delignify and brighten kraft pulps. To better understand the mechanism of this biological bleaching and the by-products formed, I traced the transformation of pulp lignin during treatment with the fungus. Hardwood and softwood kraft pulps containing 14C-labelled residual lignin were prepared by laboratory pulping of lignin-labelled aspen and spruce wood and then incubated with T. versicolor. After initially polymerizing the lignin, the fungus depolymerized it to alkali-extractable forms and then to soluble forms. Most of the labelled carbon accumulated in the water-soluble pool. The extractable and soluble products were oligomeric; single-ring aromatic products were not detected. The mineralization of the lignin carbon to CO2 varied between experiments, up to 22% in the most vigorous cultures. The activities of the known enzymes laccase and manganese peroxidase did not account for all of the lignin degradation that took place in the T. versicolor cultures. This fungus may produce additional enzymes that could be useful in enzyme bleaching systems.