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 |