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

≥500 U/g

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in Aspergillus oryzae

Quality Level

form

beads (powder like)
beads

specific activity

≥500 U/g

storage temp.

2-8°C

General description

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 in adsorption kinetics studies using Quartz crystal microbalance with dissipation (QCM-D).
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.

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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Improved acylation of phytosterols catalyzed by Candida antarctica lipase A with superior catalytic activity
Panpipat W, et al.
Biochemical Engineering Journal, 70(1), 55-62 (2013)
Lipase-catalyzed synthesis of the chiral tetrahydroisoquinoline (R)-salsolinol
Ding W, et al.
Tetrahedron, 23(18-19), 1376-1379 (2012)
Orientating lipase molecules through surface chemical control for enhanced activity: a QCM-D and ToF-SIMS investigation
Joyce P, et al.
Colloids and Surfaces. B, Biointerfaces, 142, 173-181 (2016)
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)
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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