Lipases are found in pancreatic secretions. This class of enzymes contains α and β hydrolase folds. Candida rugosa produces multiple lipase isoenzymes that have 80% sequence homology.
Lipases can be used in a wide range of solvents, in both aqueous and non-aqueous media, and thus have found use in applications like organic synthesis.
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.
Lipase from Candida rugosa has been used:
- to synthesize dextran fatty acid esters
- to study the effect of lipase on conjugated linoleic acid (CLA1 and CLA2) production in the presence of sunflower oil and castor oil
- to prepare pH-imprinted enzyme for lipase-catalyzed transesterification of dextran T-40 with vinyl decanoate
5, 10, 25, 100 g in poly bottle
Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
Lipases are biocatalysts useful for biotransformation reactions. It possesses broad substrate tolerance and is highly stereo- and regioselective. Lipases mediate lipid transport. Elevated levels of serum lipase are observed in pancreatitis. Lipases are the preferred catalysts for long-chain fatty acids.
One unit will hydrolyze 1.0 microequivalent of fatty acid from a triglyceride in 1 hr at pH 7.2 at 37 °C. (This is equivalent to approx. 10 microliters of CO2 in 30 minutes.)