Lipases in water-in-ionic liquid microemulsions: Structural and activity studies

dc.contributor.authorPavlidis, I. V.en
dc.contributor.authorGournis, D.en
dc.contributor.authorPapadopoulos, G. K.en
dc.contributor.authorStamatis, H.en
dc.date.accessioned2015-11-24T17:35:23Z
dc.date.available2015-11-24T17:35:23Z
dc.identifier.issn1381-1177-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/14119
dc.rightsDefault Licence-
dc.subjectlipaseen
dc.subjectionic liquidsen
dc.subjectmicroemulsionsen
dc.subjectstabilityen
dc.subjectft-iren
dc.subjectcircular dichroismen
dc.subjectchromobacterium-viscosum lipaseen
dc.subjectisooctane reverse micellesen
dc.subjectsecondary structureen
dc.subjectcircular-dichroismen
dc.subjecthumicola-lanuginosaen
dc.subjectenzymatic-reactionsen
dc.subjectthermal-stabilityen
dc.subjectorganic-solventsen
dc.subjectcandida-rugosaen
dc.subjectmediaen
dc.titleLipases in water-in-ionic liquid microemulsions: Structural and activity studiesen
heal.abstractWater-in-ionic liquid (w/IL) microemulsions formulated with non-ionic surfactants, (Tween 20 or Triton X-100) in 1-butyl-3-methylimidazolium hexafluorophosphate ([bmim]PF(6)), were used as media for lipase-catalyzed esterification reactions. The catalytic behavior and stability of lipases from Candida rugosa, Chromobacterium viscosum and Thermomyces lanuginosa in these novel microemulsions were investigated and compared to other microheterogeneous media used so far for enzyme-catalyzed reactions. The catalytic behavior of the enzymes depends strongly on the surfactant concentration and the water content. The dependence of the esterification activity of lipases on molar ratio of water to surfactant (w(o)) follows a bell-shaped profile, presenting a maximum at w(o) approximate to 5. The operational stability of lipases in w/IL microemulsions, especially at high incubation temperature (50 degrees C), was significantly increased compared to that observed in other microheterogeneous media. The highest half-life times (>100 h) were obtained in w/IL microemulsions with low water content. Conformational studies via Fourier transform-infrared (FT-IR) and circular dichroism (CD) spectroscopy indicated that lipases entrapped in w/IL microemulsions in most cases retain their native structure or adapt a more rigid structure compared to other microheterogeneous media, which correlated well with the stability results. A simple procedure suitable for ester separation and enzyme reuse was developed. T lanuginosa lipase retained 90% of activity after ten reaction cycles in w/IL microemulsions formulated with Tween 20. (C) 2009 Elsevier B.V. All rights reserved.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDOI 10.1016/j.molcatb.2009.03.007-
heal.identifier.secondary<Go to ISI>://000267248700007-
heal.journalNameJournal of Molecular Catalysis B-Enzymaticen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2009-
heal.publisherElsevieren
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Μηχανικών Επιστήμης Υλικώνel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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