Studies on the catalytic behaviour of a cholinesterase-like abzyme in an AOT microemulsion system

Franqueville, E; Stamatis, H; Loutrari, H; Friboulet, A; Kolisis, F

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	2014-03-01T01:18:22Z
dc.date.available	2014-03-01T01:18:22Z
dc.date.issued	2002	en
dc.identifier.issn	0168-1656	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/14963
dc.subject	AOT surfactant	en
dc.subject	Catalytic antibody	en
dc.subject	Isooctane	en
dc.subject	Reverse micelle	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	Catalysis	en
dc.subject.other	Fluorescence	en
dc.subject.other	Hydrolysis	en
dc.subject.other	Micelles	en
dc.subject.other	Microemulsions	en
dc.subject.other	Monoclonal antibodies	en
dc.subject.other	Sodium compounds	en
dc.subject.other	Surface active agents	en
dc.subject.other	Molar ratio	en
dc.subject.other	Enzymes	en
dc.subject.other	abzyme	en
dc.subject.other	acetic acid derivative	en
dc.subject.other	acetylcholinesterase	en
dc.subject.other	docusate sodium	en
dc.subject.other	enzyme	en
dc.subject.other	octane	en
dc.subject.other	surfactant	en
dc.subject.other	unclassified drug	en
dc.subject.other	water	en
dc.subject.other	aqueous solution	en
dc.subject.other	article	en
dc.subject.other	catalysis	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme substrate	en
dc.subject.other	fluorescence	en
dc.subject.other	hydrolysis	en
dc.subject.other	kinetics	en
dc.subject.other	micelle	en
dc.subject.other	microemulsion	en
dc.subject.other	priority journal	en
dc.subject.other	productivity	en
dc.subject.other	Animals	en
dc.subject.other	Antibodies, Catalytic	en
dc.subject.other	Antibodies, Monoclonal	en
dc.subject.other	Catalysis	en
dc.subject.other	Cholinesterases	en
dc.subject.other	Dioctyl Sulfosuccinic Acid	en
dc.subject.other	Emulsions	en
dc.subject.other	Enzyme Stability	en
dc.subject.other	Enzymes, Immobilized	en
dc.subject.other	Hydrolysis	en
dc.subject.other	Immunoglobulin M	en
dc.subject.other	Mice	en
dc.subject.other	Micelles	en
dc.subject.other	Nitrobenzenes	en
dc.subject.other	Octanes	en
dc.subject.other	Oils	en
dc.subject.other	Phenylacetates	en
dc.subject.other	Reproducibility of Results	en
dc.subject.other	Sensitivity and Specificity	en
dc.subject.other	Solubility	en
dc.subject.other	Substrate Specificity	en
dc.subject.other	Surface-Active Agents	en
dc.subject.other	Water	en
dc.title	Studies on the catalytic behaviour of a cholinesterase-like abzyme in an AOT microemulsion system	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/S0168-1656(02)00061-5	en
heal.identifier.secondary	http://dx.doi.org/10.1016/S0168-1656(02)00061-5	en
heal.language	English	en
heal.publicationDate	2002	en
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.publisher	ELSEVIER SCIENCE BV	en
heal.journalName	Journal of Biotechnology	en
dc.identifier.doi	10.1016/S0168-1656(02)00061-5	en
dc.identifier.isi	ISI:000177080000007	en
dc.identifier.volume	97	en
dc.identifier.issue	2	en
dc.identifier.spage	177	en
dc.identifier.epage	182	en