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Improving the catalytic performance of fungal laccases in monoterpene-based reaction systems

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dc.contributor.author Tzialla, AA en
dc.contributor.author Taha, AA en
dc.contributor.author Kalogeris, E en
dc.contributor.author Stamatis, H en
dc.date.accessioned 2014-03-01T01:30:53Z
dc.date.available 2014-03-01T01:30:53Z
dc.date.issued 2009 en
dc.identifier.issn 0141-5492 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/19668
dc.subject Laccases en
dc.subject Stabilization en
dc.subject Ternary systems en
dc.subject Terpenes en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other Botrytis cinerea en
dc.subject.other Catalytic efficiencies en
dc.subject.other Catalytic performance en
dc.subject.other D-limonene en
dc.subject.other Fungal laccases en
dc.subject.other Laccases en
dc.subject.other Monoterpenes en
dc.subject.other Non-conventional media en
dc.subject.other Reaction media en
dc.subject.other Reaction system en
dc.subject.other Residual enzymes en
dc.subject.other Terpenes en
dc.subject.other Tert butanol en
dc.subject.other Trametes versicolor en
dc.subject.other Catalysts en
dc.subject.other Enzyme activity en
dc.subject.other Enzymes en
dc.subject.other Lipids en
dc.subject.other Olefins en
dc.subject.other Reaction rates en
dc.subject.other Stabilization en
dc.subject.other Water content en
dc.subject.other Ternary systems en
dc.subject.other Botryotinia fuckeliana en
dc.subject.other Fungi en
dc.subject.other Trametes versicolor en
dc.subject.other fungal protein en
dc.subject.other laccase en
dc.subject.other solvent en
dc.subject.other terpene en
dc.subject.other tert butyl alcohol en
dc.subject.other water en
dc.subject.other article en
dc.subject.other Botrytis en
dc.subject.other chemistry en
dc.subject.other enzyme stability en
dc.subject.other enzymology en
dc.subject.other isolation and purification en
dc.subject.other metabolism en
dc.subject.other temperature en
dc.subject.other time en
dc.subject.other Trametes en
dc.subject.other Botrytis en
dc.subject.other Enzyme Stability en
dc.subject.other Fungal Proteins en
dc.subject.other Laccase en
dc.subject.other Monoterpenes en
dc.subject.other Solvents en
dc.subject.other Temperature en
dc.subject.other tert-Butyl Alcohol en
dc.subject.other Time Factors en
dc.subject.other Trametes en
dc.subject.other Water en
dc.title Improving the catalytic performance of fungal laccases in monoterpene-based reaction systems en
heal.type journalArticle en
heal.identifier.primary 10.1007/s10529-009-0014-5 en
heal.identifier.secondary http://dx.doi.org/10.1007/s10529-009-0014-5 en
heal.language English en
heal.publicationDate 2009 en
heal.abstract Ternary systems consisting of monoterpenes (α-pinene or D-limonene), tert-butanol and water were used as reaction media to enhance the catalytic performance of laccases from various fungi sources (Trametes versicolor, T. hirsuta and Botrytis cinerea). The enzymes had improved catalytic efficiency (5- to 10-fold) in α-pinene-rich environment, while optimal reaction rates were in high-water content systems (15.5% v/v). The stability of laccases was significantly improved in monoterpene-based systems (up to 90% residual enzyme activity after 24 h at 30°C) in comparison with other non-conventional media. The results indicate that these ternary systems can increase the potential of laccases as catalysts for various oxidations. © Springer Science+Business Media B.V. 2009. en
heal.publisher SPRINGER en
heal.journalName Biotechnology Letters en
dc.identifier.doi 10.1007/s10529-009-0014-5 en
dc.identifier.isi ISI:000268726500021 en
dc.identifier.volume 31 en
dc.identifier.issue 9 en
dc.identifier.spage 1451 en
dc.identifier.epage 1456 en


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