Candida antarctica lipase B (CalB) is structurally similar to several other lipases and has a flexible lid. It is made up of 317 amino acids and has a molecular weight of 33 kDa. Lipase B is a member of the alpha/beta hydrolase-fold family.

Lipase B Candida antarctica, recombinant from Aspergillus oryzae has been used:

• as a standard to characterize the enzymatic properties of D5-CalB
• as an efficient biocatalyst to start the reaction to obtain (R)-ester via esterification of racemic secondary alcohol
• to investigate a “green” recycling route for polybutylene succinate (PBS) based on reactive extrusion
• to compare the esterification yield with adsorbed CaLB (aCaLB) and covalently immobilized CaLB (cCaLB)

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 catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
Candida antarctica lipase B (CALB) possesses wide substrate specificity, high activity and high enantioselectivity, hence it is considered as a major enzyme in biotechnology. It also has the capability to perform in aqueous and non-aqueous reaction environments. CALB is used in transesterification, kinetic resolution and polymerization reactions.

1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 8.0 and 40°C (tributyrin, Cat. No. 91010, as substrate)