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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Franqueville, E. | en |
| dc.contributor.author | Stamatis, H. | en |
| dc.contributor.author | Loutrari, H. | en |
| dc.contributor.author | Friboulet, A. | en |
| dc.contributor.author | Kolisis, F. | en |
| dc.date.accessioned | 2015-11-24T16:32:43Z | - |
| dc.date.available | 2015-11-24T16:32:43Z | - |
| dc.identifier.issn | 0168-1656 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7580 | - |
| dc.rights | Default Licence | - |
| dc.subject | catalytic antibody | en |
| dc.subject | reverse micelle | en |
| dc.subject | aot surfactant | en |
| dc.subject | isooctane | en |
| dc.subject | reverse micelles | en |
| dc.subject | bioorganic reactions | en |
| dc.subject | antibody catalysis | en |
| dc.subject | organic-solvents | en |
| dc.subject | lipases | en |
| dc.subject | enzymes | en |
| dc.title | Studies on the catalytic behaviour of a cholinesterase-like abzyme in an AOT microemulsion system | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://000177080000007 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.publicationDate | 2002 | - |
| heal.abstract | The hydrolytic activity of a monoclonal catalytic antibody (9A8) (abzyme) with acetylcholinesterase-like activity was investigated in water-in-oil (w/o) microemulsions (reverse micelles) based on sodium his-2-(ethylhexyl)sulfosuccinate (AOT) in isooctane, using p- and o-nitrophenylacetate (p-and o-NPA) as substrates. The dependence of the abzyme hydrolytic activity on the molar ratio of water to surfactant (w(o)) showed a bell-shaped curve, presenting a maximum at w(o) = 11.1. An increase of the AOT concentration at constant w(o), resulted in a decrease of the catalytic activity suggesting a possible inhibition effect of the surfactant. The incorporation of the abzyme into the reverse micelle system caused a blue shift of the fluorescence emission maximum by a magnitude of 7-10 nm depending on the w(o) value. This result indicates that the antibody molecule, or a large part of it, is located in the aqueous tnicrophase of the system. Kinetic studies showed that the hydrolysis of p-and o-NPA in microemulsion system as well as in aqueous solution follows Michaelis-Menten kinetics. The catalytic efficiency (k(cat)/K-m) in w/o microemulsion was significant lower than in aqueous solution. (C) 2002 Elsevier Science B.V. All rights reserved. | en |
| heal.journalName | Journal of Biotechnology | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| stamatis-2002-Studies on the catalytic behaviour of a cholinesterase-like abzyme in an AOT microemulsion system.pdf | 112.15 kB | Adobe PDF | View/Open Request a copy |
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