41658
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
NACRES:
NA.54
UNSPSC Code:
12352204
Specific activity:
≥500 U/g
Recombinant:
expressed in Aspergillus oryzae
recombinant
expressed in Aspergillus oryzae
form
beads (powder like), beads
specific activity
≥500 U/g
storage temp.
2-8°C
Quality Level
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.
Other Notes
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
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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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
The acyltransferase activity of lipase CAL-A allows efficient fatty acid esters formation from plant oil even in an aqueous environment
Muller J, et al.
European Journal of Lipid Science and Technology, 117(12), 1903-1907 (2015)
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)
Biocatalysis as a profound tool in the preparation of highly enantiopure β-amino acids
A. Liljeblad, L.T. Kanerva
Tetrahedron, 62, 5831-5854 (2006)
X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation
Ericsson D, et al.
Journal of molecular biology, 376(1), 109-119 (2008)
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