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52583

Sigma-Aldrich

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

≥2000 U/g

Sinónimos:

Candida antarctica Lipase

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in yeast

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)

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)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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)
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)
Asymmetric Morita-Baylis-Hillman reaction catalyzed by pepsin
Xue JW, et al.
Journal of Molecular Catalysis. B, Enzymatic, 124, 62-69 (2016)
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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