Pseudomonas cepacia lipase: Esterification reactions in AOT microemulsion systems

dc.contributor.authorStamatis, H.en
dc.contributor.authorXenakis, A.en
dc.contributor.authorBornscheuer, U.en
dc.contributor.authorScheper, T.en
dc.contributor.authorMenge, U.en
dc.contributor.authorKolisis, F. N.en
dc.date.accessioned2015-11-24T16:35:02Z
dc.date.available2015-11-24T16:35:02Z
dc.identifier.issn0141-5492-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7890
dc.rightsDefault Licence-
dc.subjectBiomedical and Life Sciencesen
dc.titlePseudomonas cepacia lipase: Esterification reactions in AOT microemulsion systemsen
heal.abstractSummary The activity of purified Pseudomonas cepacia lipase has been investigated in esterification reactions of various aliphatic alcohols with natural fatty acids. The reactions were carried out in microemulsions formed in isooctane by bis(2ethylhexyl)sulfosuccinate sodium salt (AOT). The optima pH, T and water content (w o ) for the enzyme activity in this type of microemulsions have been determined. Studies on the effect of various fatty acids and alcohols on the enzyme specificity have shown a preference of this lipase for palmitic and caprylic acid as well as for propanol, while reactions involving cyclic alcohols can not be catalyzed at all. The differences on the behavior of this lipase as compared to other lipases studied in microemulsion systems as well as in other systems are discussed.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1007/bf01080143-
heal.identifier.secondaryhttp://dx.doi.org/10.1007/BF01080143-
heal.journalNameBiotechnology Lettersen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1993-
heal.publisherSpringer Netherlandsen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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