Lipase catalytic ability to hydrolyze triglycerides and phospholipids

CARELLI, AMALIA ANTONIA; GUTIÉRREZ AYESTA, CECILIA; FERREIRA, MARÍA LUJÁN

Madrid

Congreso; 4th European Federation for the Science and Technology of Lipid Congress; 2006

Lipases with different kinds of active sites were investigated for their catalytic ability to hydrolyze sunflower oil, soybean lecithin, their artificial mixtures and sunflower gum for six hours in heptane at 60°C and pH 7.0. Conversions were highly dependent on the selected lipase. Lipolase 100 T, which is a granulated silica-immobilized commercial Humicola lanuginosa lipase, exhibited the highest conversion to fatty acids (100%) when the oil and its mixture with lecithin were tested. These studies revealed that lipases, whose active sites are on the surface, present the major activity in the substrate coordination. Besides, lipases whose active sites are like a funnel or like a tunnel had some difficulties to coordinate the substrate and therefore showed a lower conversion.