A rise in the hydrolysis activity of Candida rugosa lipase caused by pressurized treatment with supercritical carbon dioxide

The hydrolysis activity of Candida rugosa lipase (lipase OF) treated with supercritical CO., was measured. The activity of the lipase, which was treated for one hour at 308.15 K and 19.61 MPa, is approximately 2.5 times higher than that of the untreated lipase. Changes in the content of proteins in the lipase and also in the size of the lipase particle after treatment were investigated through fluorescence emission spectra meter and scanning electron microscopy respectively. The size reduction of particles and the purification of the enzyme might be the main reasons for the increase in Candida rugosa lipase's activity.