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About This Item
NACRES:
NA.54
UNSPSC Code:
12352204
Specific activity:
≥2000 U/g
Recombinant:
expressed in yeast
recombinant
expressed in yeast
Quality Segment
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
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.
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.
Other Notes
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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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