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Pseudomonas cepacia lipase localization in lecitihin and AOT w/o microemulsions. a fluorescence energy transfer study

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dc.contributor.author Avramiotis, S en
dc.contributor.author Stamatis, H en
dc.contributor.author Kolisis, FN en
dc.contributor.author Xenakis, A en
dc.date.accessioned 2014-03-01T01:46:06Z
dc.date.available 2014-03-01T01:46:06Z
dc.date.issued 1997 en
dc.identifier.issn 0340255X en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/24850
dc.relation.uri http://www.scopus.com/inward/record.url?eid=2-s2.0-0344256216&partnerID=40&md5=fcd315d513c35a87bdcbad513aab849d en
dc.subject Lecithin en
dc.subject Lipase en
dc.subject Microemulsions en
dc.subject Reverse micelles en
dc.title Pseudomonas cepacia lipase localization in lecitihin and AOT w/o microemulsions. a fluorescence energy transfer study en
heal.type journalArticle en
heal.publicationDate 1997 en
heal.abstract Two water-in-oil microemulsion systems formulated with lecithin and AOT were used to solubilize lipase from Pseudomonas cepacia. The site of localization of the enzyme within the different microdomains of the dispersed phase was investigated by applying the fluorescence energy transfer technique. The nonradiative energy transfer from the tryptophan residues of lipase to an adequate acceptor molecule, such as cis-parinaric acid, was studied in both systems. The effect of the water content of the microemulsions, as well as the effect of the molar ratio of lipase to cis-parinaric acid was examined. The results showed that in both microemulsion systems lipase is preferentially localized near the surfactant membrane and that in the case of the lecithin-based systems the interface is less penetrable than the AOT one. en
heal.journalName Progress in Colloid and Polymer Science en
dc.identifier.volume 105 en
dc.identifier.spage 180 en
dc.identifier.epage 183 en


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