Please cite this article in press as: M. de Cazes, et al., Design and optimization of an enzymatic membrane reactor for tetracycline degradation, Catal. Today (2014), http://dx.doi.org/10.1016/j.cattod.2014.02.051 ARTICLE IN PRESS G Model CATTOD-8952; No. of Pages 7 Catalysis Today xxx (2014) xxx–xxx Contents lists available at ScienceDirect Catalysis Today j our na l ho me page: www.elsevier.com/locate/cattod Design and optimization of an enzymatic membrane reactor for tetracycline degradation M. de Cazes a , M.-P. Belleville a , E. Petit a , M. Llorca b , S. Rodríguez-Mozaz b , J. de Gunzburg c , D. Barceló b,d , J. Sanchez-Marcano a, a Université de Montpellier 2, Institut Européen des Membranes, UMR 5635 (CNRS-ENSCM-UM2), CC 047, 2 Place Eugène Bataillon, 34095 Montpellier Cedex 5, France b Catalan Institute for Water Research (ICRA), Scientific and Technological Park of the University of Girona, H2O building, C/Emili Grahit 101, E-17003 Girona, Spain c Da Volterra, Le Dorian, building B1, 172 rue de Charonne, 75011 Paris, France d Water and Soil Quality Research Group, Dept. of Environmental Chemistry, IDAEA-CSIC, Jordi Girona 18-26, 08034 Barcelona, Spain a r t i c l e i n f o Article history: Received 29 July 2013 Received in revised form 23 October 2013 Accepted 10 February 2014 Available online xxx Keywords: Enzymatic membrane reactor Active membrane Laccase Tetracycline Wastewater treatment Micropollutant degradation a b s t r a c t The tetracycline, antibiotic considered as a recalcitrant pollutant, was successfully depleted from model aqueous solutions by immobilized laccase from Trametes versicolor in an enzymatic membrane reactor. The results obtained show that tetracycline is depleted from water solutions at room temperature and without adding any extra chemicals. The degradation of tetracycline in aqueous solutions at 20 mg L -1 during 24 h, with equivalent amounts of free or immobilized biocatalyst, allowed reaching a tetracycline degradation yield of 56% with an enzymatic membrane whereas it was only of 30% with free laccase. This result highlights the good reactivity and stability of the immobilized enzyme for the degradation of tetracycline. Moreover, the enzymatic membrane reactor was able to reach a constant degradation rate of 0.34 mg of tetracycline per hour during 10 days. © 2014 Elsevier B.V. All rights reserved. 1. Introduction With the background of an aging population and increasing urbanization, pharmaceutical products (PPs) and endocrine dis- rupting chemicals (EDCs) have been continuously released in the environment for a long time without being considered as priority pollutants to target. As conventional wastewater treatment technologies are not effi- cient enough to completely remove pharmaceuticals from water, such products are currently found in water effluents from sewage facilities, as well as in surface water, in groundwater, adsorbed on sediments and even in drinking water [1–3]. Furthermore, ecotox- icity studies have demonstrated that PPs could affect the growth, reproduction and behavior of birds, fishes, invertebrates, plants and bacteria [4–6]. In particular, the presence of low concentra- tions of antibiotics in wastewaters could cause the development of Corresponding author. Tel.: +33 467 149 149/+33 467 1419; fax: +33 467 149 119. E-mail address: sanchez@iemm.univ-montp2.fr (J. Sanchez-Marcano). antibiotic resistance by bacteria and then be an important source of public health problems in the future [7]. Indeed, lately important research efforts have been done in order to find a system to eliminate the PPs before rejecting the effluents to the environment. Among the different processes tested (physical adsorption, chemical or biological reactions) for the depletion of certain groups of pollutants [8–12], the use of bio- catalysts such as laccases, glycosylases, proteases and lipases have been found to be particularly efficient [13]. In particular laccases are able to oxidize a wide range of pollutants at room temperature within a large range of pH using as oxidant the oxygen dissolved in water. Consequently, some reports have noticed the potential of laccase-catalyzed reactions for the removal of a large spectrum of pollutants [14–19]. To overcome the drawbacks related to enzymes cost, biocata- lysts can be immobilized on a large variety of supports [16,18] as well as in membranes and used in enzymatic membrane reactors (EMRs) [20–22]. In EMRs the substrate solution flows through the membrane to the biocatalyst as a result of transmembrane pres- sure. Then the reaction takes place simultaneously with the mass transfer process through the membrane and the product is recov- ered in the permeate. Thus a precise control of the reaction with http://dx.doi.org/10.1016/j.cattod.2014.02.051 0920-5861/© 2014 Elsevier B.V. All rights reserved.