Kauffmann, C., Kennedy Leigh Ctr. for Hort. Res., Otto Warburg Ctr. Agric. Biotech., Hebrew University of Jerusalem, P.O. Box 12, Rehovot 76100, Israel
Shoseyov, O., Kennedy Leigh Ctr. for Hort. Res., Otto Warburg Ctr. Agric. Biotech., Hebrew University of Jerusalem, P.O. Box 12, Rehovot 76100, Israel
Shpigel, E., CBD-Technologies Ltd., Park Tamar, 2 Pekeris Street, Rehovot 76100, Israel
Bayer, E.A., Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Lamed, R., Dept. Molec. Microbiol. and Biotech., Tel-Aviv University, Ramat Aviv 69978, Israel
Shoham, Y., Dept. of Food Eng. and Biotechnology, Technion - IIT, Haifa 32000, Israel
Mandelbaum, R.T., Inst. Soil, Water and Environ. Sci., Volcani Research Institute, Bet Dagan 50250, Israel

s-Triazines including atrazine are heavily used agricultural herbicides, and their extensive removal from industrial wastewater is required before these effluents can be disposed. The use of enzymes for this purpose is an important potential alternative to conventional methods of detoxification. The purpose of the present study was to develop an enzyme-based technology for the treatment of atrazine contaminated water. In this paper we describe the construction and expression of two fusion proteins which dechlorinate atrazine while being firmly bound to an insoluble cellulose matrix. Dechlorination of atrazine produces in one enzymatic step the nonregulated compound hydroxyatrazine from the regulated mother compound, atrazine.