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Merck

62288

Sigma-Aldrich

Lipase B Candida antarctica, recombinant from Aspergillus oryzae

powder, beige, ~9 U/mg

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About This Item

Número de CAS:
Comisión internacional de enzimas:
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

signalword

Danger

hcodes

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)


Certificados de análisis (COA)

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Visite la Librería de documentos

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)
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)
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)
A novel self-activation mechanism of Candida antarctica lipase B
Luan B and Zhou R
Physical Chemistry Chemical Physics, 19(24), 15709-15714 (2017)

Artículos

Efficient epimerization catalyst for enzyme mediated dynamic kinetic resolution (DKR).

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