Sahin, OzlemErdemir, SerkanUyanik, ArzuYilmaz, Mustafa2020-03-262020-03-2620090926-860X1873-3875https://dx.doi.org/10.1016/j.apcata.2009.08.030https://hdl.handle.net/20.500.12395/23511Lipases are enzymes that catalyses a variety of reactions, such esterifications, interesterification and hydrolysis. Several methods have been reported for the immobilization of lipases, such as deposition onto solid supports, covalent binding and encapsulation within a polymer matrix or silica glasses obtained by sol-gel techniques. In this study, the Candido rugosa lipase was encapsulated within a chemically inert sol-gel support prepared by polycondensation by tetraetoxysilane (TEOS)and octyltrietoxysilane(OTES) in the presence and absence of calix[n]arene, calix[n]-NH2 and calix[n]-COOH (n = 4,6,8) compounds as additives. The catalytic activity of the encapsulated lipases was evaluated into model reactions, i.e. the hydrolysis of p-nitrophenylpalmitate (p-NPP), and the enantioselective hydrolysis of rasemic Naproxen methyl ester that was studied in aqueous buffer solution/isooctane reaction system. The results indicated that the particularly calix[4,6]-NH2 and calix[6]-COOH based encapsulated lipases had higher conversion and enantioselectivity compared to the sol-gel free lipase. (C) 2009 Elsevier B.V. All rights reserved.en10.1016/j.apcata.2009.08.030info:eu-repo/semantics/closedAccessCalixarenesEnzymeEncapsulationEnantioselectivitySol-gelArticle36901.02.20203641Q1WOS:000271689600005Q1