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41658

Sigma-Aldrich

Lipase A Candida antarctica immobilized on Immobead 150, recombinant from Aspergillus oryzae

≥500 U/g

Synonym(s):

Candida antarctica Lipase

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in Aspergillus oryzae

form

beads (powder like)
beads

specific activity

≥500 U/g

storage temp.

2-8°C

General description

Research area: Cellsignalling. Lipase A Candida Antarctica, CalA is a thermostable, calcium-dependent enzyme with high substrate specificity. CalA comprises of the catalytic triad (Ser184, Asp334, His366) and has an α/β hydrolase structural fold.

Application

Lipase A Candida antarctica immobilized on Immobead 150, recombinant from Aspergillus oryzae has been used in the synthesis of enantiopure (R)-salsolinol and adsorption kinetics studies using Quartz crystal microbalance with dissipation (QCM-D).It has also been used tostudy the esterification of difluorinated alcohols.
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Biochem/physiol Actions

Lipase A Candida Antarctica, CalA is highly specific for alcohols and esterifies the trans-isomer of fatty acids. CalA recognizes highly branched acyl groups and is active on alcohols with steric hindrance. CalA catalyzes the production of enantiopure amino acids and aids in the synthesis of chiral cyanohydrins. It may find industrial applications for its thermostable functionality in paper industry.Lipase A Candida antarctica(CAL-A) shows acetyltransferase activity by synthesizing fatty acid esters from certain alcohols and natural oils in an aqueous environment.

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 10.0 and 40°C (tributyrin, Cat. No. 91010, as substrate)

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Daniel J Ericsson et al.
Journal of molecular biology, 376(1), 109-119 (2007-12-25)
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty acids. Under the appropriate conditions, the reaction is reversible, and so biotechnological applications commonly make use of their capacity for esterification as well as for
High yield expression of Lipase A from Candida antarctica in the methylotrophic yeast Pichia pastoris and its purification and characterisation
Pfeffer J, et al.
Applied Microbiology and Biotechnology, 72(5), 931-931 (2006)
Biocatalysis as a profound tool in the preparation of highly enantiopure β-amino acids
A. Liljeblad, L.T. Kanerva
Tetrahedron, 62, 5831-5854 (2006)
Karel Pomeisl et al.
Bioorganic & medicinal chemistry, 27(7), 1246-1253 (2019-02-20)
An enzymatic alternative to the chemical synthesis of chiral gem-difluorinated alcohols has been developed. The method is highly effective and stereoselective, feasible at laboratory temperature, avoiding the use of toxic heavy metal catalysts which is an important benefit in medicinal
Biotechnological applications of Candida antarctica lipase A: State-of-the-art
de Maria PD, et al.
Journal of Molecular Catalysis. B, Enzymatic, 37(1-6), 36-46 (2005)

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