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62288

Sigma-Aldrich

Lipase B Candida antarctica, recombinant from Aspergillus oryzae

powder, beige, ~9 U/mg

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CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
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

Regulatory Information

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. What solvent can Lipase B Candida antarctica, recombinant from Aspergillus oryzae, Product 62288, be dissolved in?

    Lipase B is expected to be soluble in water. We are able to dissolve the enzyme in water for the enzymatic assay. We also have tested the solubility of Lipase B in 0.05M potassium phosphate buffer solution (pH=7.5) during quality control at a concentration of 10mg/mL. According to the chemicals encyclopedia published by the Royal Society of Chemistry, almost all organic solvents decrease lipase activity, with the exception of petroleum ether.  

  4. Is Product 62288, Lipase B Candida antarctica, recombinant from Aspergillus oryzae, lyophilized?

    This lipase is a lyophilisate and may contain Gum arabic for adjustment of activity. The amount of Gum arabic in each vial is lot dependent.

  5. How pure is Product 62288, Lipase B Candida antarctica, recombinant from Aspergillus oryzae?

    Purity is not determined for this product. As is the case with many of our enzymes, the product is assayed for enzymatic activity, not for purity.

  6. What is the molecular weight of Lipase B Candida antarctica, recombinant from Aspergillus oryzae, Product 62288?

    Unfortunately, molecular weight information is unavailable at this time.

  7. What is Product 62288, Lipase B Candida antarctica, recombinant from Aspergillus oryzae, soluble in?

    Lipase B is expected to be soluble in water. We are able to dissolve the enzyme in water for the enzymatic assay. We also have tested the solubility of Lipase B in 0.05 M potassium phosphate buffer solution (pH=7.5) during quality control at a concentration of 10 mg/mL. According to the chemicals encyclopedia published by the Royal Society of Chemistry, almost all organic solvents decrease lipase activity, with the exception of petroleum ether.

  8. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  9. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  10. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

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

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