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Laccase Immobilisation on Mesostructured Silicas

100%
Bryjak J., Szymańska K., Jarzębski A. B.
Chemical and Process Engineering
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2012
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vol. 33
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issue 4
611-620
EN
Extracellular laccase produced by the wood-rotting fungus Cerrena unicolor was immobilised covalently on the mesostructured siliceous foam (MCF) and three hexagonally ordered mesoporous silicas (SBA-15) with different pore sizes. The enzyme was attached covalently via glutaraldehyde (GLA) or by simple adsorption and additionally crosslinked with GLA. The experiments indicated that laccase bound by covalent attachment remains very active and stable. The best biocatalysts were MCF and SBA-15 with Si-F moieties on their surface. Thermal inactivation of immobilised and native laccase at 80°C showed a biphasic-type activity decay, that could be modelled with 3- parameter isoenzyme model. It appeared that immobilisation did not significantly change the mechanism of activity loss but stabilised a fraction of a stable isoform. Examination of time needed for 90% initial activity loss revealed that immobilisation prolonged that time from 8 min (native enzyme) up to 155 min (SBA-15SF).
2
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Purification and characterization of a novel laccase from the mushroom Pleurotus nebrodensis

100%
Tian G.-T., Zhang G.-Q., Wang H.-X., Ng T. B.
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2012
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vol. 59
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issue 3
407-412
EN
A novel laccase with a molecular mass of 64 kDa and the N-terminal sequence AIGPDDTINF was isolated from fresh fruiting bodies of the mushroom Pleurotus nebrodensis. The purification protocol comprised ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration on Superdex 75. The laccase was adsorbed on DEAE-cellulose and Q-Sepharose, but not on CM-cellulose. It demonstrated an optimal temperature of 70°C. The enzyme activity increased steadily over the temperature range 20°C-70°C. There was only a slight reduction in activity at 80°C. However, all activity disappeared following exposure to 100°C for 10 minutes. The enzyme activity changed only slightly over the pH range 3-5, with the optimum at pH 5, but underwent a precipitous decline when the pH was elevated to 6, and was undetectable at pH 8 and pH 9.
3
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Fungal laccases as tools for biodegradation of industrial dyes

100%
Zucca P., Cocco G., Sollai F., Sanjust E.
Biocatalysis
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2014
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vol. 1
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issue 1
EN
Laccases are blue copper oxidases, found in some plants and secreted by a wide range of ligninolytic fungi. These enzymes are well known for their ability in oxidizing several organic compounds, mainly phenolics and aromatic amines, at the expenses of molecular oxygen. Therefore, they could find application in the field of enzymatic bioremediation of many industrial wastewaters, and in particular to bleach and/or detoxify dye-containing effluents. Not all industrial dyes behave as laccase substrates, but this limitation is often overcome by the judicious use of redox mediators. These could substantially widen the application range of laccases as bioremediation tools. The present study encompasses the main properties of the most used industrial dyes as related to their chemical classification, fungal laccases and their molecular and catalytic features, the use of redox mediators, limitations and perspectives of the use of fungal laccases for industrial dye bleaching.
4
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Laccase Immobilisation on Mesostructured Silicas

88%
Bryjak J., Szymańska K., Jarzębski A. B.
Chemical and Process Engineering
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2012
|
issue 4
5
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Laccase concentration by foam fractionation of Cerrena unicolor and Pleurotus sapidus culture supernatants

88%
Blatkiewicz M., Ledakowicz S., Antecka A., Górak A.
Chemical and Process Engineering
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2017
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vol. 38
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issue 3
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