Activity and stability studies of Mucor miehei lipase immobilized in novel microemulsion-based organogels
| dc.contributor.author | Delimitsou, C. | en |
| dc.contributor.author | Zoumpanioti, M. | en |
| dc.contributor.author | Xenakis, A. | en |
| dc.contributor.author | Stamatis, H. | en |
| dc.date.accessioned | 2015-11-24T16:32:42Z | |
| dc.date.available | 2015-11-24T16:32:42Z | |
| dc.identifier.issn | 1024-2422 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7578 | |
| dc.rights | Default Licence | - |
| dc.subject | microemulsions | en |
| dc.subject | organogel | en |
| dc.subject | lipase | en |
| dc.subject | esterification | en |
| dc.subject | kinetics | en |
| dc.subject | immobilization | en |
| dc.subject | in-oil microemulsions | en |
| dc.subject | chromobacterium-viscosum lipase | en |
| dc.subject | organic-solvents | en |
| dc.subject | catalyzed esterification | en |
| dc.subject | enzyme immobilization | en |
| dc.subject | bioorganic reactions | en |
| dc.subject | gels | en |
| dc.subject | gelatin | en |
| dc.subject | kinetics | en |
| dc.title | Activity and stability studies of Mucor miehei lipase immobilized in novel microemulsion-based organogels | en |
| heal.abstract | Lipase from Mucor miehei was immobilized in bis-(2-ethylhexyl)sulfosuccinate sodium salt MOT) as well as lecithin water-in-oil (w/o) microemulsion-based organogels (MBGs) formulated with biopolymers such as agar and hydroxypropylmethyl cellulose (HPMC), respectively. These lipase-containing MBGs prove to be novel solid-phase catalysts for use in organic media. Using these organogels at 25degreesC, various esterification reactions in non-polar solvents as well as in solvent free systems were possible. Apparent lipase activity was influenced to some extent by the nature and the concentration of biopolymers used. Lipase stability in such MBGs is much higher than that observed in w/o microemulsions. MBGs containing lipase functioned effectively in repeated batch syntheses of fatty esters. Kinetic studies have shown that ester synthesis catalyzed by immobilized lipase occurs via the Ping-Pong bi-bi mechanism in which only inhibition by excess of alcohol has been identified. Values of all kinetic parameters were determined. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | Doi 10.1080/10242420290025539 | - |
| heal.identifier.secondary | <Go to ISI>://000178518900003 | - |
| heal.identifier.secondary | http://informahealthcare.com/doi/abs/10.1080/10242420290025539 | - |
| heal.journalName | Biocatalysis and Biotransformation | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2002 | - |
| 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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