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54326

Sigma-Aldrich

Lipase B Candida antarctica immobilized on Immobead 150, recombinant from Aspergillus oryzae

≥1800 U/g

Synonym(s):

Candida lipase, Immobilized lipase, Recombinant lipase

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (Candida antarctica)

Quality Level

100

recombinant

expressed in Aspergillus oryzae

form

beads

specific activity

≥1800 U/g

technique(s)

analytical sample preparation: suitable

color

white to off-white

application(s)

life science and biopharma

storage temp.

2-8°C

Gene Information

fungus ... LIPB(1170790)

General description

Research area: Cell Signaling

Lipase B from Candida antarctica (CAL-B) is a serine hydrolase, α/β-hydrolase, and is a member of the lipase family. CAL-B is composed of an α/β-hydrolase fold and the active site contains a Ser-His-Asp catalytic triad.

Application

Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Biochem/physiol Actions

Lipase B from Candida antarctica (CAL-B) acts as a catalyst for producing amines, amides, and alcohols.. It is used as a biocatalyst in research and industry. CAL-B is involved in the hydrolysis of triglycerides. Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.

Unit Definition

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 Code

11 - Combustible Solids

WGK

WGK 3

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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Interfacial activation of Candida antarctica lipase B: combined evidence from experiment and simulation
Themistoklis Z, et al.
Biochemistry, 54(38), 5969?5979- 5969?5979 (2015)
Biotechnological relevance of the lipase A from Candida antarctica
Monteiro RRC, et al.
Catalysis Today, 362, 141-154 (2021)
Karel Pomeisl et al.
Bioorganic & medicinal chemistry, 27(7), 1246-1253 (2019-02-20)
An enzymatic alternative to the chemical synthesis of chiral gem-difluorinated alcohols has been developed. The method is highly effective and stereoselective, feasible at laboratory temperature, avoiding the use of toxic heavy metal catalysts which is an important benefit in medicinal

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