Lipase B Candida antarctica immobilized on Immobead 150, recombinant from yeast

Lipase B or triacylglycerol ester hydrolases belongs to the class of hydrolases. Lipase B from Candida antarctica (CALB) possesses 317 amino acids and a molecular weight of 33 kDa. CALB has a catalytic triad and an open solvent accessible active site. The catalytic triad is usually Ser-His-Asp/Glu which is found in the carboxy terminal of parallel β sheet.

Lipase B Candida antarctica immobilized on Immobead 150, recombinant from yeast has been used:

• in esterification reaction of lauric acid with n-butanol in a biphasic solvent system
• in hydrolysis of fish oil triglycerides
• in screening of enzymes for Morita–Baylis–Hillman (MBH) reaction

Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Lipase B from Candida antarctica has been shown to be an effective catalyst for the synthesis of esters of ethyl D-glucopyranoside from fatty acids larger than octanoic acid. It has also been found to catalyze a wide variety of organic reactions including many different regio- and enantio-selective syntheses.

Lipases B from Candida antarctica (CALB) is a versatile catalyst for biotransformation reactions. In aqueous media, CALB behaves like an esterase rather than a lipase.

Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.

1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 7.5 and 40°C (tributyrin, Cat. No. 91010, as substrate)