62288
Lipase B Candida antarctica, recombinant from Aspergillus oryzae
powder, beige, ~9 U/mg
recombinant
expressed in Aspergillus oryzae
Quality Level
form
powder
specific activity
~9 U/mg
mol wt
33 kDa
color
beige
storage temp.
2-8°C
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-;
InChI key
QWZUIMCIEOCSJF-CHHCPSLASA-N
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General description
Candida antarctica lipase B (CalB) is structurally similar to several other lipases and has a flexible lid. It is made up of 317 amino acids and has a molecular weight of 33 kDa. Lipase B is a member of the alpha/beta hydrolase-fold family.
Application
Lipase B Candida antarctica, recombinant from Aspergillus oryzae has been used:
- as a standard to characterize the enzymatic properties of D5-CalB
- as an efficient biocatalyst to start the reaction to obtain (R)-ester via esterification of racemic secondary alcohol
- to investigate a “green” recycling route for polybutylene succinate (PBS) based on reactive extrusion
- to compare the esterification yield with adsorbed CaLB (aCaLB) and covalently immobilized CaLB (cCaLB)
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 catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
Candida antarctica lipase B (CALB) possesses wide substrate specificity, high activity and high enantioselectivity, hence it is considered as a major enzyme in biotechnology. It also has the capability to perform in aqueous and non-aqueous reaction environments. CALB is used in transesterification, kinetic resolution and polymerization reactions.
Candida antarctica lipase B (CALB) possesses wide substrate specificity, high activity and high enantioselectivity, hence it is considered as a major enzyme in biotechnology. It also has the capability to perform in aqueous and non-aqueous reaction environments. CALB is used in transesterification, kinetic resolution and polymerization reactions.
Other Notes
1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 8.0 and 40°C (tributyrin, Cat. No. 91010, as substrate)
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Simple amino acid tags improve both expression and secretion of Candida antarctica lipase B in recombinant Escherichia coli
Kim S K, et al.
Biotechnology and Bioengineering, 112(2), 346-355 (2015)
Sun-Ki Kim et al.
Biotechnology and bioengineering, 112(2), 346-355 (2014-09-04)
Escherichia coli is the best-established microbial host strain for production of proteins and chemicals, but has a weakness for not secreting high amounts of active heterologous proteins to the extracellular culture medium, of which origins belong to whether prokaryotes or
Structural behavior of Candida antarctica lipase B in water and supercritical carbon dioxide: A molecular dynamic simulation study
Housaindokht M R, et al.
Journal of Supercritical Fluids, 63, 180-186 (2012)
A green method for polybutylene succinate recycling: Depolymerization catalyzed by lipase B from Candida antarctica during reactive extrusion
Jbilou F, et al.
European Polymer Journal, 68, 207-215 (2015)
A novel self-activation mechanism of Candida antarctica lipase B
Luan B and Zhou R
Physical Chemistry Chemical Physics, 19(24), 15709-15714 (2017)
Articles
Efficient epimerization catalyst for enzyme mediated dynamic kinetic resolution (DKR).
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