26-27 mai 2025 - Pôle API - Illkirch-Graffenstaden (France)
Optimization of acetylcholinesterase immobilization monitored with a rapid and specific colorimetric technique
Paul Bresson, Yue Ma, Diane Julien-David, Eric Marchioni  1@  
1 : Equipe de Chimie Analytique des Molécules BioActives, Université de Strasbourg, CNRS, IPHC UMR 7178  (Institut Pluridisciplinaire Hubert Curien)
CNRS : UMR7178
74 route du Rhin, 67400 Illkirch-Graffenstaden -  France

The goal of this work was to optimize the conditions for acetylcholinesterase immobilization on different stationary phases and to monitor the immobilization reaction using a rapid technique. This procedure will enable the construction of an immobilized enzyme reactor for use in enzyme inhibitor screening. For this study, amino silica (NUCLEODUR 100 - 5μm NH2) and a monolithic disk (CIM, 7.9mm x 2.1mm, aldehyde-coated) were used. The enzyme immobilization was carried out in batch and the reaction was monitored by evaluating the activity of the residual acetylcholinesterase in solution using Ellman's assay. The influence of the enzyme-to-stationary phase ratio was tested. It was shown that the grafting reaction occurred rapidly on both types of media. It was also demonstrated that a greater amount of acetylcholinesterase could be immobilized on the CIM disk before saturation



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