Journal of Molecular Catalysis B: Enzymatic 22 (2003) 119–133 Preparation and properties of lipase immobilized on MCM-36 support Emil Dumitriu a,∗ , Francesco Secundo b , Joël Patarin c , Ioana Fechete a a Laboratory of Catalysis, Technical University of Iasi, 71 D. Mangeron, Iasi 6600, Romania b Istituto di Chimica del Riconoscimento Molecolare, v. Mario Bianco 9, 20131 Milan, Italy c Laboratoire de Matériaux Minéraux, Université de Haute Alsace, 3 rue Alfred Werner, 68093 Mulhouse, France Received 30 January 2003; accepted 30 January 2003 Abstract Based on pure MCM-22 precursor, MCM-36 was produced by swelling and pillaring with SiO 2 pillars. These materials were characterized by X-ray diffraction (XRD), scanning electron microscopy (SEM), thermogravimetric analysis/differential scanning calorimetry (TGA/DSC), MAS NMR, and N 2 adsorption isotherms. Compared with the MCM-22 sample, the resulting MCM-36 material contains a mesoporous region between the microporous layers, with a mesopore volume of 0.472 cm 3 /g, and the surface area increased up to 671 m 2 /g. Lipase from Candida antarctica B (CALB) was immobilized on both supports by physical adsorption at equilibrium. Twenty milligrams of CALB/g of MCM-22 was adsorbed on the external surface of crystals, while only 4 mg CALB/g support was adsorbed onto the mesoporous hybrid material MCM-36. The mechanism of adsorption was also discussed. The acylation of alcohols (1-butanol and 1-octanol) by vinyl esters (vinyl acetate and vinyl stearate) was used as a test reaction in order to evaluate the catalytic activity of MCM-36-immobilized lipase. The test reaction indicated MCM-36-immobilized enzyme as an active catalyst for the acylation and its activity was approximately two times higher than that of the free lipase (for the vinyl acetate/1-butanol system). © 2003 Elsevier Science B.V. All rights reserved. Keywords: Enzyme immobilization; Lipase; Acylation; MCM-22 zeolite; MCM-36 1. Introduction A distinguishing feature of the recent developments in organic synthesis is an emphasis upon the selec- tivity. At the same time, in the last years the control of stereochemistry, and in particular the formation of only one optical isomer (enantioselectivity), is one of the most active areas of research because of its prime importance in the synthesis of fine chemicals, mainly for pharmaceutical and agrochemical products. The ∗ Corresponding author. Tel.: +40-232-278-683; fax: +40-232-271-311. E-mail address: edumitri@ch.tuiasi.ro (E. Dumitriu). experimental data indicated enzymes as very attrac- tive and useful catalysts for both purposes, because enzymes can accept and transform selectively not only natural substrates but also foreign synthetic substrates in both aqueous solutions and organic solvents under mild conditions. Among hydrolases, the lipases are often used because they are inexpensive and easy to handle for synthetic organic chemists. Other reasons for the enor- mous interest with regard to the use of lipases as bio- catalysts include: (i) they are stable in organic solvents, (ii) do not require cofactors, (iii) possess broad sub- strate specificity, (iv) exhibit a high enantioselectivity [1]. The biological function of lipases is to catalyze 1381-1177/03/$ – see front matter © 2003 Elsevier Science B.V. All rights reserved. doi:10.1016/S1381-1177(03)00015-8