52583
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
Recommended Products
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)
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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