TY - JOUR AB - The objective of this work was to produce an immobilized form of lipase from Burkholderia cepacia (lipase PS) with advantageous catalytic properties and stability to be used in the ethanolysis of different feedstocks, mainly babassu oil and tallow beef. For this purpose lipase PS was immobilized on two different non-commercial matrices, such as inorganic matrix (niobium oxide, Nb(2)O(5)) and a hybrid matrix (polysiloxane-polyvinyl alcohol, SiO(2)-PVA) by covalent binding. The properties of free and immobilized enzymes were searched and compared. The best performance regarding all the analyzed parameters (biochemical properties, kinetic constants and thermal stability) were obtained when the lipase was immobilized on SiO(2)-PVA. The superiority of this immobilized system was also confirmed in the transe-sterification of both feedstocks, attained higher yields and productivities. (C) 2010 Elsevier Ltd. All rights reserved. AD - Univ Sao Paulo, Engn Sch Lorena, BR-12602810 Sao Paulo, Brazil AN - WOS:000277581100063 AU - Da Ros, P. C. M. AU - Silva, G. A. M. AU - Mendes, A. A. AU - Santos, J. C. AU - de Castro, H. F. DA - Jul DO - 10.1016/j.biortech.2010.02.061 IS - 14 J2 - Bioresource Technol KW - lipase LA - English N1 - 594zs PY - 2010 SN - 0960-8524 SP - 5508-5516 ST - Evaluation of the catalytic properties of Burkholderia cepacia lipase immobilized on non-commercial matrices to be used in biodiesel synthesis from different feedstocks T2 - Bioresource Technology TI - Evaluation of the catalytic properties of Burkholderia cepacia lipase immobilized on non-commercial matrices to be used in biodiesel synthesis from different feedstocks UR - ://WOS:000277581100063 VL - 101 ID - 5399 ER -