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73940

Sigma-Aldrich

Lipase immobilized from Candida antarctica

beads, slightly brown, >2 U/mg

Synonym(s):

Immobilized Lipase, Lipase Enzyme

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About This Item

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

form

beads

Quality Level

specific activity

>2 U/mg

color

slightly brown

density

2 g/mL at 20 °C

storage temp.

2-8°C

General description

Lipases belong to the class of hydrolases. Microbes of plant and animal basis mainly produce lipase enzyme. It can also be produced by marine organisms.

Application

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

Biochem/physiol Actions

Lipases are used in detergent, food, leather, pharmaceutical and dairy industries. It has several characteristics like substrate specificity, stereospecificity and regioselectivity. It also participates in various bioconversion reactions like, hydrolysis, esterification, acidolysis and aminolysis.
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 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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Marine fungal and bacterial isolates for lipase production: A comparative study
Advances in Food and Nutrition Research, 78, 71-94 (2016)
Lipase: An Industrial Enzyme Through Metagenomics
Lipase: An Industrial Enzyme Through Metagenomics (2018)
J Hall et al.
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