Esterification reactions of lipase in reverse micelles
dc.contributor.author | Hayes, Douglas G. | en_US |
dc.contributor.author | Gulari, Erdogan | en_US |
dc.date.accessioned | 2006-04-28T16:30:19Z | |
dc.date.available | 2006-04-28T16:30:19Z | |
dc.date.issued | 1990-04-05 | en_US |
dc.identifier.citation | Hayes, 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.issn | 0006-3592 | en_US |
dc.identifier.issn | 1097-0290 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/37904 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=18592580&dopt=citation | en_US |
dc.description.abstract | The 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.extent | 902586 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Biochemistry and Biotechnology | en_US |
dc.title | Esterification reactions of lipase in reverse micelles | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbsecondlevel | Mathematics | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Statistics and Numeric Data | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Social Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemical Engineering, The University of Michigan, Room 3074 H. H. Dow Building, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Department 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 48109 | en_US |
dc.identifier.pmid | 18592580 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/37904/1/260350807_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/bit.260350807 | en_US |
dc.identifier.source | Biotechnology and Bioengineering | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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