Esterification reactions catalyzed by lipases in microemulsions: The role of enzyme localization in relation to its selectivity
| dc.contributor.author | Stamatis, H. | en |
| dc.contributor.author | Xenakis, A. | en |
| dc.contributor.author | Provelegiou, M. | en |
| dc.contributor.author | Kolisis, F. N. | en |
| dc.date.accessioned | 2015-11-24T16:35:03Z | |
| dc.date.available | 2015-11-24T16:35:03Z | |
| dc.identifier.issn | 1097-0290 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7893 | |
| dc.rights | Default Licence | - |
| dc.subject | lipases | en |
| dc.subject | selectivity | en |
| dc.subject | esterifications | en |
| dc.subject | microemulsions | en |
| dc.subject | reverse micelles | en |
| dc.title | Esterification reactions catalyzed by lipases in microemulsions: The role of enzyme localization in relation to its selectivity | en |
| heal.abstract | The activity of lipases from Rhizopus delemar, Rhizopus arrhizus, and Penicillium simplicissimum entrapped in microemulsions formulated by bis-(2-ethylhexyl)sulfo-succinate sodium salt (AOT) in isooctane has been studied in esterification reactions of various aliphatic alcohols with fatty acids. The effect of the nature of the fatty acids (chain length) and of the alcohols (primary, secondary, or tertiary; chain length; cyclic structures) on the lipase activities was investigated in relation to the reverse micellar structure. The lipases tested showed a selectivity regarding the structure of the substrates used when hosted in the AOT/isooctane microemulsion systems. Penicillium simplicissimum lipase showed higher reaction rates in the esterification of long chain alcohols as well as secondary alcohols. Primary alcohols had a low reaction rate and tertiary a very slow rate of esterification. Long chain fatty acids were better catalyzed as compared to the shorter ones. Rhizopus delemar and R. arrhizus lipases showed a preference for the esterification of short chain primary alcohols, while the secondary alcohols had a low rate of esterification and the tertiary ones could not be converted. The reaction of medium chain length fatty acids was also better catalyzed than in the case of the long ones. The observed lipase selectivity appeared to be related to the localization of the enzyme molecule within the micellar microstructure due to the hydrophobic/hydrophilic character of the protein. The reverse micellar structural characteristics, as well as the localization of the enzyme, were examined by fluorescence quenching measurements and spectroscopical studies. Β© 1993 John Wiley & Sons, Inc. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | 10.1002/bit.260420114 | - |
| heal.identifier.secondary | http://dx.doi.org/10.1002/bit.260420114 | - |
| heal.journalName | Biotechnol Bioeng | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 1993 | - |
| heal.publisher | Wiley Subscription Services, Inc., A Wiley Company | en |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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