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dc.contributor.advisorLitthauer, D.
dc.contributor.advisorVan Tonder, A.
dc.contributor.advisorWolfaardt, F.
dc.contributor.authorBar, Marièlle
dc.date.accessioned2015-07-22T13:13:24Z
dc.date.available2015-07-22T13:13:24Z
dc.date.issued2001-12
dc.identifier.urihttp://hdl.handle.net/11660/649
dc.description.abstractLaccase (EC 1.10.3.2, p-diphenol oxidase) is one of a few enzymes that have been studied since the nineteenth century. Yoshida first described laccase in 1883 when he extracted it from the exudates of the Japanese lacquer tree, Rhus vernicifera. (Thurston, 1994; Levine, 1965). In 1896 laccase was demonstrated to be a fungal enzyme for the first time by both Bertrand and Laborde (Thurston, 1994; Levine, 1965). Laccase is a member of the large blue copper proteins or blue copper oxidases, which comprise a small group of enzymes. Other enzymes in this group are the plant ascorbate oxidases and the mammalian plasma protein ceruloplasmin (Thurston, 1994; Xu, 1996; Ducros et al., 1998). Laccases are either mono or multimeric copper-containing oxidases that catalyse the one-electron oxidation of a vast amount of phenolic substrates. Molecular oxygen serves as the terminal electron acceptor and is thus reduced to two molecules of water (Ducros et al., 1998). The ability of laccases to oxidise phenolic compounds as well as their ability to reduce molecular oxygen to water has lead to intensive studies of these enzymes (Jolivalt et al., 1999; Xu, 1996; Thurston, 1994). The biotechnological importance of these enzymes can also be attributed to their substantial retention of activity in organic solvents with applications in organic synthesis. Laccases have widespread applications, ranging from effluent decolouration and detoxification to pulp bleaching, removal of phenolics from wines and dye transfer blocking functions in detergents and washing powders, many of which have been patented (Yaver et al., 2001). The biotechnological application of laccase has been expanded by the introduction of laccase- mediator systems, which are able to oxidise non-phenolic compounds that are otherwise not attacked and are thus able to degrade lignin in kraft pulps (Bourbonnais and Paice, 1990).en_ZA
dc.language.isoenen_ZA
dc.publisherUniversity of the Free Stateen_ZA
dc.subjectLignin -- Biodegradationen_ZA
dc.subjectBasidiomycetesen_ZA
dc.subjectOxidoreductasesen_ZA
dc.subjectLaccasesen_ZA
dc.subjectFungalen_ZA
dc.subjectWhite-roten_ZA
dc.subjectPhysico-chemical propertiesen_ZA
dc.subjectKineticsen_ZA
dc.subjectDissertation (M.Sc. (Microbiology and Biochemistry))--University of the Free State, 2002
dc.titleKinetics and physico-chemical properties of white-rot fungal laccasesen_ZA
dc.typeDissertationen_ZA
dc.rights.holderUniversity of the Free Stateen_ZA


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