Merck, 62288-50MG-F, Lipase B Candida antarctica, recombinant from Aspergillus oryzae

General description
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.
Application
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.
Biochem/physiol Actions
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.
Other Notes
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)