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
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.
Lipase B from Candida antarctica has been shown to be an effective catalyst for the synthesis of esters of ethyl
Unit Definition
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)
- UPC:
- 51302402
- Condition:
- New
- Weight:
- 1.00 Ounces
- HazmatClass:
- No
- WeightUOM:
- LB
- MPN:
- 62288-50MG-F