Assembly strategies for enzyme immobilization

POLY 391

Mark Lambermon,, Linda JA Hendriks,, Sanne Schoffelen,, Matthijn Vos, m.r.j.vos@tue.nl2, Nikos S. Hatzakis,, NoŽlle Carette, carette@bordeaux.inra.fr3, Alan E. Rowan,, Jeroen J. L. M. Cornelissen,, Thierry Michon, michon@bordeaux.inra.fr3, Nico A. J. M. Sommerdijk, N.Sommerdijk@tue.nl2, and Jan C. M. van Hest, (1) Department of Organic Chemistry, Radboud University Nijmegen, Toernooiveld 1, Nijmegen, 6525 ED, Netherlands, (2) Laboratory of Macromolecular and Organic Chemistry, Eindhoven University of Technology, Den Dolech 2, 5600 MB Eindhoven, Netherlands, (3) Laboratory of plant virology, IBVM-INRA Bordeaux, BP 81, Villenave d'Ornon, 33883, France, (4) Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, Netherlands, (5) Department of Organic Chemistry, Nijmegen University, Toernooiveld 1, 6525 ED Nijmegen, Netherlands
Nature's ability to perform cascade reactions in an effective way is based on the correct assembly of the different biocatalysts in a metabolon. Positional control is especially important in multistep reactions, in which the product of one catalytic reaction is used directly as substrate for the next transformation. We are developing scaffolds for enzyme immobilization to produce synthetic metabolons. These scaffolds are based on self assembling organized systems. We are using virus particles and aggregates formed in water by an ammonium terminated surfactant, in which a bis-ureido group is incorporated in its hydrocarbon chain. In addition we are engineering a model enzyme (Candida antarctica lipase B) so that it harbors functionalities that can be used to covalently link the enzyme to such structures in a bio orthogonal manner.

Biocatalysis in Polymer Science
1:30 PM-4:45 PM, Tuesday, 12 September 2006 San Francisco Marriott -- Salon 12/13, Oral

Division of Polymer Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006