Kinetic Study of Hepatic Triglyceride Lipase from Rat Liver Soluble Fraction

Abstract

An assay is described for the determination of lipase activity, using as substrate an emulsion of radioactive triolein with cholic acid as emulsifier. Lipase activity is given by determining radioactive triolein disappearance after incubation with the artificial emulsion. The catalytic activity of this enzyme has been studied with respect to time, protein concentration and substrate concentration. Under the experimental conditions, Michaelis constant value was 14.54 mmol/1 and maximal hydrolysis rate 0.31 μmol h^-1 mg^-1.

A Short Review on Various Screening Methods to Isolate Potential Lipase Producers: Lipases-the Present and Future Enzymes of Biotech Industry

“…For quantification, TLC can be followed by a densitometric or autoradiographic analysis (using radio labeled TAGs) of the fatty acid bands. These techniques offer high specificity and sensitivity and can be used to detect the released fatty acids as low as pico moles (Ruiz-Larrea et al, 1981). The major problems concerned to these techniques include time-consumption and they are not continuous.…”