Although several enzymes presumed to be part of the delignification/kraft pulp biobleaching system of the white-rot basidiomycete Trametes versicolor have been studied, characterized, and even exploited as pulp treatments, the complete system remains poorly understood. Little is known about which enzymes are essential for delignification, how they are regulated, or whether there remain unknown enzymes essential to wood decay in this system. Auxotrophic mutants of T. versicolor 52J were developed and characterized. Plasmid pUC18 was complemented with the T. versicolor 52J genome to create a gene library. Transformation with this plasmid-gene library converted argB and ade2 auxotrophs of T. versicolor 52J to prototrophy. Attempts to rescue the plasmids responsible were unsuccessful. Several different pre-existing plasmid constructs were examined for their potential as selectable markers on the fungus. One of these, pGPhT, worked well at conferring phleomycin resistance. Given that there are now available partial or complete sequences for four T. versicolor laccases, the single cellobiose dehydrogenase, and a lignin peroxidase isozyme, these genetic tools should be very useful in dissecting the mechanisms of white-rot delignification.

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A thesis submitted in fulfillment of the requirement for the Degree Master of Technology: Biotechnology, M.L. Sultan technikon, 2000. / The ever-increasing demand for a wide variety of paper products has led to the pulp and paper industry becoming one of the largest industries in the world. In 1988 the United States alone produced almost 71 million metric tonnes of paper and pulp board (Jeffries, 1992). South Africa has also become one of the major international producers of pulp and paper products. Since 1970, the production of paper and board by the South African industry achieved an average growth rate of 5.2% per annum, and in 1997 South Africa was the twelfth largest producer of pulp and 24th biggest supplier of paper and board in the world (Molony, 1999 / M

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Submitted in fulfillment of the requirements of the degree of Master of Technology (Biotechnology), Durban University of Technology, Durban, South Africa, 2014. / Microbial enzymes are gaining worldwide attention due to their potential industrial applications. Microorganisms producing thermostable -xylanase and their associated hemicellulases have significant application in the paper and pulp, food, animal feed, and textile industries. The potential of partially purified xylanase from Thermomyces lanuginosus MC 134, Luminase PB 100, Luminase PB 200 (a commercial xylanase) and T. lanuginosus DSM 5826 (Sigma Aldrich) was evaluated in bleaching of bagasse pulp. The temperature and pH optima for all the enzymes were 60°C and pH 6, respectively. The temperature (50- 80°C) and pH (5-8) stability of the enzymes were also assessed. All the enzymes were relatively stable at 60°C and pH 6 for 180 min. T. lanuginosus MC 134 retained 80% of its activity at 60°C and pH 6 for 180 min and PB 200 retained 75% of its activity at 80°C for 180 min. T. lanuginosus MC 134 also exhibited good alkaline stability at pH 8. The commercial xylanases Luminase PB 100, Luminase PB 200, T. lanuginosus DSM 5826 (Sigma Aldrich) were purified to homogeneity using a gel filtration column packed with sephadex G-100 and characterized for Km and Vmax. However extracellular crude xylanases from T. lanuginosus MC 134 was purified to homogeneity using (N )2S04 precipitation and gel filtration column, packed with sephadex G-100. The purified xylanases exhibited a molecular mass of- 26 to 24 kDa, given range as determined by SDS page. The Km and Vmax values of Luminase PB 100, Luminase PB 200, T. lanuginosus MC 134, and T. lanuginosus DSM 5826, xylanases were determined by the Michaelis-Menten equation using birchwood xylan as the substrate. The Km value for Luminase PB 100, Luminase PB 200, T. lanuginosus DSM 5826 and T. lanuginosus MC 134 were, 8.1 mg/mL, 11.7 mg/mL and 14.3 mg/mL respectively. The Vmax for Luminase PB 100, Luminase PB 200, T lanuginosus DSM 5826 and T lanuginosus MC 134 were 232.6, 454.6 and 74.6 !Jl11ol/min/mg. Biobleaching conditions of the xylanases were also optimised and the release of reducing sugars and lignin derived compounds showed that an enzyme dosage of 50U/g of pulp was ideal for biobleaching at pH 6 and 60°C for 180 min. This brightness for T lanuginosus MC 134, Luminase PB 200, Luminase PB 100 was 45.5 ± 0.11%, 44.1 ± 0.007% and 42.7 ± 0.03% respectively at pH 6, compared to untreated samples. Reducing sugars and UV-absorbing lignin-derived compound values were considerably higher in xylanase-treated samples. All the enzymes analysed exhibited similar trends in the release of lignin derived compounds and reducing sugars which indicated their potential in the pulp and paper industry. / PDF Full-text unavailable. Please refer to hard copy for Full-text / M

A series of laboratory oxygen delignification were performed in this study at constant oxygen pressure and consistency to study the response of the pulp to the different process parameters, i.e. reaction temperature, reaction time, soda addition, and mechanical pretreatment, to the zero span tensile strength loss. The basic chemistry of the oxygen delignified pulps was under study including fiber charge, celluloses/hemicelluloses, and hexenuronic acid. The fiber structure such as curl, kink, fines, and fiber length were also discussed. NaOH charge can be reduced as much as 50 % by applying mechanical pretreatment to obtain the same level of selectivity at the oxygen delignification conditions described in this study.Mechanical pretreatment prior to oxygen delignification promoted a better selectivity for both Acacia mangium and MHW pulps. MHW kraft pulp did not show a significant extractive removal in all pretreatment methods during oxygen delignification. The ultrasonic pretreatment followed by filtering induced the best extractive removal among the other three methods.

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