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In a limited screen of monokaryons and dikaryons of various strains of Trametes versicolor, the monokaryons generally bleached hardwood and softwood kraft pulps more extensively than dikaryons, although there was great variation among both groups. A monokaryotic strain (52J) derived from a Paprican dikaryon (52P) by regenerating mycelium-derived protoplasts had better pulp bleaching ability than its dikaryotic parent. Unusually low extracellular laccase and manganese peroxidase activity levels were associated with reduced pulp bleaching. Mutants of strain 52J were isolated with various manganese peroxidase and laccase activities. Those with markedly reduced laccase and manganese peroxidase activity had impaired abilities to bleach, delignify, and produce methanol from hardwood kraft pulp, mineralize $ sp{14}$C-labelled synthetic lignins, reduce the colour of kraft mill bleach plant effluent, or had lost these abilities altogether. Dechlorination of kraft bleach plant effluent organochlorines was only slightly less in the mutants tried than in 52J. When purified manganese peroxidase was added back to mutant M49 of 52J, significant pulp bleaching was restored. Effluent decolorization also improved with added manganese peroxidase.

The extracellular culture supernatants of the white rot fungus Trametes versicolor can bleach and delignify unbleached kraft pulps, however the process is too slow for commercial application. Though at least two oxidative enzymes, laccase and manganese peroxidase (MnP) produced by this organism can catalyze a partial delignification of kraft pulp, the effect observed is small relative to that obtained with the complete fungal system. To develop a synthetic (cell-free) delignification system, other protentially important components of the culture supernatant were identified and their contributions to biobleaching and delignification were evaluated. The presence of pulp did not significantly affect the overall carbon balance of the fungus, but a number of non-volatile metabolites (oxalic, fumaric, glyoxylic and phenyllactic acids) induced by the presence of pulp were identified. In T. versicolor 52J, the secretion of manganese peroxidase (MnP), and cellobiose:quinone oxidoreductase (CBQase) enzymes were inducible by pulp whereas cellulase and laccase were not. Several low molecular weight metabolites secreted by T. versicolor functioned as effective Mn(III) complexing agents at their physiological concentrations and promoted MnP activity. / Two distinct CBQase proteins are secreted by T. versicolor 52J, CBQase 4.2 a a 113kDa homodimer containing both heme and flavin cofactors and CBQase 6.4, a 48 kDa monomer with a flavin cofactor only. Superficially, these enzymes appear very similar to the cellobiose oxidase (CBO) and CBQase reported in Phanerochaete chrysosporium. CBQase 4.2 was shown to reduce insoluble manganese dioxide to its soluble Mn(II) and Mn(III) forms with the concommitant oxidation of cellobiose. The sugar acids formed by CBQase could function as effective complexing agents for Mn(III),and complement the Mn(II) to Mn(III) oxidation activity of MnP. / It is proposed that a redox cycling of lignin molecules by certain fungal oxidative and reductive enzymes occurs during delignification and that this cycling ultimately promotes net lignin degradation. A redox cycle wa established between T. versicolor CBQase and laccase which allowed the O$ sb2$ comsumption rate of laccase to remain at a constant level and the total O$ sb2$ consumption by the enzyme was much treater than if the substrate were incubated with laccase alone. A new assay for CBQase based on the ability of this enzyme to reduce the radical intermediates formed during laccase-mediated chlorpromazine oxidation was developed. A redox cycle for these two enzymes was established using both model substrates like CPZ, and with a kraft lignin preparation. CBQase inhibited the formation of polymeric material by laccase; however no evidence was found indicating that cycling with these two enzymes favors depolymerization of kraft lignin. However, the alkali extractability of residual lignin in kraft pulp was increased by a sequential treatment with MnP followed by CBQase.

The work described in this dissertation was aimed at obtaining an understanding of / Thesis (M.Sc.Eng.)-University of KwaZulu-Natal, Durban, 2007

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