Spelling suggestions: "subject:"lignin biodegradation"" "subject:"lignin diodegradation""
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The biodegradation of lignin and related aromatic compounds by basidiomycete fungiDurrant, Alastair J. January 1989 (has links)
No description available.
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Synthesis and Oxidation of Lignin-Carbohydrate Model CompoundsNguyen, Mai Thanh Thi January 2008 (has links) (PDF)
No description available.
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Biosulphidogenic hydrolysis of lignin and lignin model compoundsMadikane, Mzekelo January 2002 (has links)
Lignin degradation under biosulphidogenic conditions has not been extensively reported in the literature. Although aerobic degradation of lignin is well documented, anaerobic biodegradation has focused mainly on methanogenic systems with biosulphidogenic systems receiving less attention. Sulphate reducing bacteria are known to generate moderately high levels of both sulphide and alkalinity at room temperatures, and these conditions draw some comparison with the Kraft pulping process. In the Kraft pulping process, lignin is degraded chemically at ±170°C under high sulphide and alkaline conditions and may provide a model for understanding biosulphidogenic lignin degrading activity. The aim of this study was to investigate the biosulphidogenic hydrolysis of lignin within the context of the chemical and biological conditions generated by a mixed sulphate reducing bacteria consortia. Bioreactor studies with a mixed sulphate reducing consortia and pine wood powder (both untreated and depectinated) resulted in the generation of comparable levels of sulphide and alkalinity used in the chemical hydrolysis studies. Aromatic compound yields were between 20 to 50% of the chemical hydrolysis studies. This fluctuation may have been due to the utilization of these aromatic compounds as electron donors by the sulphate reducing consortia as evidenced by the high rate of sulphate reduction in both the untreated and depectinated wood bioreactors. Biodegradation of lignin model compounds was investigated in order to elucidate lignin degradation mechanisms. Both mono-aromatic and dimeric lignin model compounds were used as electron donors and carbon sources for the mixed sulphate reducing consortia. Biodegradation and mass spectrometer analysis of mono-aromatic compounds, ferulic acid and ferulic acid ethyl ester resulted in the production of intermediates such as catechol, cyclohexane carboxylic acid and adipic acid. These intermediates were also observed in the degradation of dimeric ferulic acid. Biodegradation of salicin resulted in the production of salicyl alcohol, ortho-cresol and acetate. Biodegradation of benzylic ether resulted in the production of vanillin and acetate as end products. The results of these studies provide evidence for a biosulphidogenic hydrolysis of lignin, and also the utilisation of lignin-derived aromatic compounds as electron donor sources, by a mixed sulphate reducing consortia.
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Biomimetic studies related to lignin degradationCui, Futong January 1990 (has links)
Lignin is the second most abundant biopolymer on Earth. It is an amorphous, cross-linked, aromatic polymer composed of phenylpropanoid units. There has been an ever growing interest in the biodegradation of this complex polymer for the last 30 years. White-rot fungi have been found to be an important lignin degraders in the natural environment. With the discovery of two groups of hemoprotein enzymes, lignin peroxidases and manganese(II)-dependent peroxidases, from the lignin degrading culture of a white-rot fungus, Phanerochaete chrysosporium, rapid progress has been made in understanding the mechanism of lignin biodegradation.
Synthetic metaUoporphyrins, the iron(III) and manganese(III) complexes of meso-tetra(2,6-dichloro-3-sulfonatophenyl)porphyrin (TDCSPPFeCl and TDCSPPMnCl) and meso-tetra(2,6-dichloro-3-sulfonatophenyl)-B-octachloroporphyrin (Cl₁₆TSPPFeCl and Cl₁₆TSPPMnCl), were used in this study to mimic the functions of the "lignin degrading" enzymes. Factors affecting the catalytic activities of these biomimetic catalysts were studied. TDCSPPFeCl could closely mimic lignin peroxidase in the degradation of a number of lignin model compounds, including veratryl alcohol, B-l, B-O-4, B-5, 5-5' biphenyl, phenylpropane, and phenylpropene model compounds. The reactions catalyzed by TDCSPPFeCl include benzyl alcohol oxidation, C[formula omitted],-C[formula omitted] side chain cleavage, demethoxylation, aromatic ring cleavage, benzylic methylene hydroxylation, and C[formula omitted]-C[formula omitted] double bond hydroxylation (glycol formation). Novel solvent incorporated compounds isolated from the oxidation of veratryl alcohol give insights about the site of attack of substrate cation radical by solvent molecules. The isolation of a solvent incorporated product from the oxidation of a phenylpropene model compound suggests a cation radical mechanism for the oxidation of this lignin substructure. The formation of
a number of direct aromatic ring cleavage products during the oxidation of some model compounds supports the previously proposed mechanism of aromatic ring cleavage. TDCSPPFeCl was also able to catalyze the oxidation of environmental pollutants such as pyrene and 2,4,6-trichlorophenol.
Veratryl alcohol and manganese(II)-complexes have been suggested to function as redox mediators for lignin biodegradation. Evidence has been provided to demonstrate their mediating power during electrochemical and biomimetic degradation of lignin model compounds.
In addition to the mechanistic information obtained, the successful oxidation of the model compounds suggests that metalloporphyrins can be important catalysts for the pulp and paper industry and for pollution control. / Science, Faculty of / Chemistry, Department of / Graduate
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Biological bleaching of kraft pulps by monokaryotic, dikaryotic, and mutant strains of Trametes versicolorAddleman, Katherine January 1994 (has links)
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.
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The role of reductive enzymes in Trametes versicolor-mediated kraft pulp biobleachingRoy, Brian Paul Patrick January 1994 (has links)
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.
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Toxicity and adsorbance abilities of Alcell lignin to bacteriaSitnikov, Dmitri. January 1999 (has links)
AlcellRTMlignin has been used commercially in adhesive preparation and brake pad linings and experimentally in animal feeds to reduce or eliminate diarrheal attacks in farm animals. Our study dealt with elucidating the antibacterial effect of AlcellRTMlignin. It would appear that adsorbance of E. coli cells to AlcellRTMlignin particles is not essential for destruction of the organism. / The antibacterial activity was delayed by the inclusion of Mg 2+ ions in the AlcellRTMlignin filtrate or in the enumeration medium (BHIA). Addition of bile salts to the enumeration medium (BHIA) enhanced the culturability loss of E. coli cells suspended in the filtrate of AlcellRTMlignin. Using FTIR methodology, it appears, that compounds of AlcellRTMlignin affect phospholipid-phospholipid and/or phospholipid-protein interactions in bacterial membranes, causing the patching of membrane phospholipids and proteins. / Additional studies are necessary to evaluate interactions of compounds of AlcellRTMlignin with bacterial cells.
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Molecular genetic manipulations in the white-rot fungus Trametes versicolorDosSantos, Gary P. January 2000 (has links)
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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Biological bleaching of kraft pulps by monokaryotic, dikaryotic, and mutant strains of Trametes versicolorAddleman, Katherine January 1994 (has links)
No description available.
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Toxicity and adsorbance abilities of Alcell lignin to bacteriaSitnikov, Dmitri. January 1999 (has links)
No description available.
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