Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

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 systemin hydrolysis of fish oil triglyceridesin 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.

Biochem/physiol Actions

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.

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.

General description

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.

Unit Definition

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)