Some biochemical properties of lipase from bay laurel (Laurus nobilis L.) seeds

Lipase was isolated from bay laurel (Laurus nobilis L.) seeds, some biochemical properties were determined. The bay laurel oil was used as the substrate in all experiments. The pH optimum was found to be 8.0 in the presence of this substrate. The temperature optimum was 50 degrees C. The specific activity of the lipase was found to be 296 U mg protein(-1) in optimal conditions. The enzyme activity is quite stable in the range of pH 7.0-10. The enzyme was stable for 1 h at its optimum temperature, and retained about 68% of activity at 60 degrees C during this time. K-m and V-max values were determined as 0.975 g and 1.298 U mg protein(-1), respectively. Also, storage stability and metal effect on lipolytic activity were investigated. Enzyme activity was maintained for 9, 12, and 42 days at room temperature, 4 and -20 degrees C, respectively. Ca2+, Co2+, Cu2+, Fe2+, and Mg2+ lightly enhanced bay laurel lipase activity.