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Sigma-Aldrich

Lipase B Candida antarctica, recombinant from Aspergillus oryzae

powder, beige, ~9 U/mg

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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

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.
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 8.0 and 40°C (tributyrin, Cat. No. 91010, as substrate)

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A novel self-activation mechanism of Candida antarctica lipase B
Luan B and Zhou R
Physical Chemistry Chemical Physics, 19(24), 15709-15714 (2017)
Preparation of passion fruit-typical 2-alkyl ester enantiomers via lipase-catalyzed kinetic resolution
Strohalm H, et al.
Journal of Agricultural and Food Chemistry, 58(10), 6328-6333 (2010)
Sol Cuenca et al.
Frontiers in plant science, 7, 464-464 (2016-05-06)
Elongated flexuous plant viral nanoparticles (VNPs) represent an interesting platform for developing different applications in nanobiotechnology. In the case of potyviruses, the virion external surface is made up of helically arrayed domains of the viral structural coat protein (CP), repeated
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)
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

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