Relation between lipase structures and their catalytic ability to hydrolyse triglycerides and phospholipids》.pdf

Enzyme and Microbial Technology 41 (2007) 35–43 Relation between lipase structures and their catalytic ability to hydrolyse triglycerides and phospholipids ´ ´ ∗ Cecilia Gutierrez-Ayesta, Amalia A. Carelli, Marıa L. Ferreira Planta Piloto de Ingenier´ıa Qu´ımica UNS-CONICET, La Carrindanga, km. 7, C.C. 717, 8000 Bah´ıa Blanca, Argentina Received 23 March 2006; received in revised form 16 November 2006; accepted 21 November 2006 Abstract Lipases with different structures were investigated for their catalytic ability to hydrolyse sunflower oil, soybean lecithin and their mixtures in heptane at 60 ◦C in a biphasic mixture heptane-buffer pH 7.0. Besides, the substrate adsorption mechanism was studied theoretically with the Chem 3D 5.0 Ultra program and the MM2 (Cambridge Soft) method by using trilinolein and phosphatidylcholine as system models of triglycerides and phospholipids, respectively. Lipolase 100T, a granulated silica immobilised commercial preparation of Thermomyces (formerly Humicola) lanuginosa lipase, evidenced the highest conversion to fatty acids when sunflower oil (85.3% conversion to fatty acids) and its mixture with lecithin (100 % conversion to fatty acids) were tested. The free lipase from Rhizomucor meiheir (RML) evidenced the highest activity with lecithin as substrate (35.6% conversion to fatty acids). The lipases with their active sites on the surface presented the highest strength of substrate coordination – as a decrease of steric energy. In the case of RML and the artificial mix sunflower oil–lecithin, the product distribution between MG, DG and FA was: 29.70% MG, 32.96% DG and 37.34% of fatty acids (FA). When Lipolase 10