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52583

Sigma-Aldrich

Lipase B Candida antarctica immobilized on Immobead 150, recombinant from yeast

≥2000 U/g

Synonym(s):

Candida antarctica Lipase

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in yeast

Quality Level

form

beads

specific activity

≥2000 U/g

mol wt

33 kDa

storage temp.

2-8°C

General description

Lipase B or triacylglycerol ester hydrolases belongs to the class of hydrolases. Lipase B from Candida antarctica (CALB) possesses 317 amino acids and a molecular weight of 33 kDa. CALB has a catalytic triad and an open solvent accessible active site. The catalytic triad is usually Ser-His-Asp/Glu which is found in the carboxy terminal of parallel β sheet.

Application

Lipase B Candida antarctica immobilized on Immobead 150, recombinant from yeast has been used:
  • in esterification reaction of lauric acid with n-butanol in a biphasic solvent system
  • in hydrolysis of fish oil triglycerides
  • in screening of enzymes for Morita–Baylis–Hillman (MBH) reaction

Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Biochem/physiol Actions

Lipases B from Candida antarctica (CALB) is a versatile catalyst for biotransformation reactions. In aqueous media, CALB behaves like an esterase rather than a lipase.
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
Lipase B from Candida antarctica has been shown to be an effective catalyst for the synthesis of esters of ethyl D-glucopyranoside from fatty acids larger than octanoic acid. It has also been found to catalyze a wide variety of organic reactions including many different regio- and enantio-selective syntheses.

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 7.5 and 40°C (tributyrin, Cat. No. 91010, as substrate)

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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Kinetics of acyl transfer reactions in organic media catalysed by Candida antarctica lipase B
Martinelle M and Hult K
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 1251(2), 191-197 (1995)
Asymmetric Morita-Baylis-Hillman reaction catalyzed by pepsin
Xue JW, et al.
Journal of Molecular Catalysis. B, Enzymatic, 124, 62-69 (2016)
The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
Uppenberg J, et al.
Structure, 2(4), 293-308 (1994)
Thermodynamic study of hydrolysis and esterification reactions with immobilized lipases
Sharma A, et al.
European International Journal of Science and Technology, 4, 128-136 (2015)
Fatty Acid Specificity in Lipase-Catalyzed Synthesis of Glucoside Esters
O. Kirk et al.
Biocatalysis and Biotransformation, 6, 127-134 (1992)

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