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Esterification reactions of lipase in reverse micelles

dc.contributor.authorHayes, Douglas G.en_US
dc.contributor.authorGulari, Erdoganen_US
dc.date.accessioned2006-04-28T16:30:19Z
dc.date.available2006-04-28T16:30:19Z
dc.date.issued1990-04-05en_US
dc.identifier.citationHayes, Douglas G.; Gulari, Erdogan (1990)."Esterification reactions of lipase in reverse micelles." Biotechnology and Bioengineering 35(8): 793-801. <http://hdl.handle.net/2027.42/37904>en_US
dc.identifier.issn0006-3592en_US
dc.identifier.issn1097-0290en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/37904
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=18592580&dopt=citationen_US
dc.description.abstractThe activities of lipase from Candida cylindracea and Rhizopus delemar have been investigated in water/AOT/iso-octane reverse micellar media through the use of two esterification reactions: fatty acid-alcohol esterification and glyceride synthesis. Such media promotes the occurrence of these two lipase-catalyzed reactions due to its low water content. The effect of various parameters on the activity of lipase from C. cylindracea in reverse micelles was determined and compared to results where alternate media were employed. It was observed that the structure of the media, as dictated by the type and concentration of the substrates and products and by the water/AOT ratio, w 0 , had a strong impact on enzyme activity. Strong deactivation of both typase types occurred in reverse micelles, especially in the absence of substrates and for w 0 values greater than 3.0. Glyceride synthesis was realized with lipase from R. delemar , but not with that from C. cylindracea ; the temperature and concentration of substrates and water strongly dictated the reaction rate and the percent conversion.en_US
dc.format.extent902586 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherChemistryen_US
dc.subject.otherBiochemistry and Biotechnologyen_US
dc.titleEsterification reactions of lipase in reverse micellesen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbsecondlevelMathematicsen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelStatistics and Numeric Dataen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelSocial Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemical Engineering, The University of Michigan, Room 3074 H. H. Dow Building, Ann Arbor, Michigan 48109en_US
dc.contributor.affiliationumDepartment of Chemical Engineering, The University of Michigan, Room 3074 H. H. Dow Building, Ann Arbor, Michigan 48109 ; Department of Chemical Engineering, The University of Michigan, Room 3074 H. H. Dow Building, Ann Arbor, Michigan 48109en_US
dc.identifier.pmid18592580en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/37904/1/260350807_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/bit.260350807en_US
dc.identifier.sourceBiotechnology and Bioengineeringen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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