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

 
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2002 (EN)
Studies on the catalytic behaviour of a cholinesterase-like abzyme in an AOT microemulsion system (EN)

Franqueville, E. (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών (EL)
Franqueville, E. (EN)

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)

catalytic antibody (EN)

Πανεπιστήμιο Ιωαννίνων (EL)
University of Ioannina (EN)

Journal of Biotechnology (EN)

English

2002

<Go to ISI>://000177080000007



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