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Merck
CN

62287

Lipase A Candida antarctica, recombinant from Aspergillus oryzae

powder, beige, ~2 U/mg

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About This Item

CAS Number:
9001-62-1
UNSPSC Code:
12352204
NACRES:
NA.26
EC Number:
232-619-9
EC Number:
3.1.1.3 (BRENDA, IUBMB)
MDL number:
MFCD00131509
Specific activity:
~2 U/mg
Recombinant:
expressed in Aspergillus oryzae

Key Documents

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Product Name

Lipase A Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~2 U/mg

InChI key

QWZUIMCIEOCSJF-CHHCPSLASA-N

InChI

1S/C11H9N3O2.Na/c15-8-4-5-9(10(16)7-8)13-14-11-3-1-2-6-12-11;/h1-7,16H,(H,12,14);/q;+1/b13-9-;

recombinant

expressed in Aspergillus oryzae

form

powder

specific activity

~2 U/mg

shelf life

limited shelf life, expiry date on the label

color

beige

storage temp.

2-8°C

Quality Level

100

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Application

Lipase A Candida antarctica, recombinant from Aspergillus oryzae has been used in the enzyme-catalyzed hydrolysis studies with 3-acetylthiohexanal. It has also been used as a biocatalyst to test its effect on the esterification of phytosterol with caprylic acid.

Biochem/physiol Actions

Lipase A Candida antarctica (CALA) is a thermostable serine hydrolase with a higher sn-2 preference towards triglycerides. It displays excellent activity towards large substrates as well as bulky sterically hindered tertiary alcohols.
Lipase A from Candida Antarctica catalyzes hydrolysis of tertiary alcohols to form glycerol and fatty acids and shows selectivity for the N-acylation of β-amino esters.

General description

Lipase A Candida antarctica (CALA) belongs to the α/β hydrolase family. The catalytic triad comprises Ser184, His366, and Asp334 residues.

Other Notes

1 U corresponds to the amount of enzyme which liberates 1 μmol oleic acid per minute at pH 8.0 and 40°C (triolein, Cat. No. 62314, as substrate); 1 U as described above is equivalent to ~0.15 U using trybutyrine, Cat. No. 91010, as substrate, at pH 8.0 and 70°C
Characterization

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
BCCK2856
BCCB2047
BCBW7807

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S.A. Patkar et al.
Indian Journal of Chemistry, 76-76 (1993)
Integrated enzymatic production of specific structured lipid and phytosterol ester compositions
Hellner G, et al.
Process. Biochem., 45(8), 1245-1250 (2010)
Biotechnological relevance of the lipase A from Candida antarctica
Monteiro RRC, et al.
Catalysis Today, 362, 141-154 (2021)
Anders G Sandström et al.
Protein engineering, design & selection : PEDS, 22(7), 413-420 (2009-06-11)
We herein report the first directed evolution of Candida antarctica lipase A (CalA), employing a combinatorial active-site saturation test (CAST). Wild-type CalA has a modest E-value of 5.1 in kinetic resolution of 4-nitrophenyl 2-methylheptanoate. Enzyme variants were expressed in Pichia
Hidehiko Wakabayashi et al.
Journal of agricultural and food chemistry, 51(15), 4349-4355 (2003-07-10)
The enantioselectivity of the generation of 3-mercaptohexanal and 3-mercaptohexanol, two potent sulfur-containing aroma compounds, by lipase-catalyzed hydrolysis of the corresponding 3-acetylthioesters was investigated. The stereochemical course of the kinetic resolutions was followed by capillary gas chromatography using modified cyclodextrins as
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