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L1754

Sigma-Aldrich

Lipase from Candida rugosa

Type VII, ≥700 unit/mg solid

Synonym(s):

Triacylglycerol acylhydrolase, Triacylglycerol lipase

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About This Item

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

biological source

fungus (candida rugosa)

type

Type VII

form

lyophilized

specific activity

≥700 unit/mg solid

storage condition

(Tightly closed. Dry)

technique(s)

cell based assay: suitable

color

beige
white

solubility

water: slightly soluble

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

Research area: Cell Structure

Lipases are found in pancreatic secretions. This class of enzymes contains α and β hydrolase folds. Candida rugosa produces multiple lipase isoenzymes that have 80% sequence homology.

Application

Lipase from Candida rugosa has been used:
  • to synthesize dextran fatty acid esters
  • to study the effect of lipase on conjugated linoleic acid (CLA1 and CLA2) production in the presence of sunflower oil and castor oil
  • to prepare pH-imprinted enzyme for lipase-catalyzed transesterification of dextran T-40 with vinyl decanoate

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

Biochem/physiol Actions

Lipases are enzymes and biocatalysts that catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids. They are useful for biotransformation reactions. It possesses broad substrate tolerance and is highly stereo- and regioselective. Lipases mediate lipid transport. Elevated levels of serum lipase are observed in pancreatitis. Lipases are the preferred catalysts for long-chain fatty acids. Lipases can be used in a wide range of solvents, in both aqueous and non-aqueous media, and thus have found use in applications like organic synthesis.
Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).

Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.

Unit Definition

One unit will hydrolyze 1.0 microequivalent of fatty acid from a triglyceride in 1 hr at pH 7.2 at 37 °C. (This is equivalent to approx. 10 microliters of CO2 in 30 minutes.)

enzyme

Product No.
Description
Pricing

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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Ashok Kumar et al.
Biological procedures online, 18, 2-2 (2016-01-15)
Lipases are industrial biocatalysts, which are involved in several novel reactions, occurring in aqueous medium as well as non-aqueous medium. Furthermore, they are well-known for their remarkable ability to carry out a wide variety of chemo-, regio- and enantio-selective transformations.
Taresh P Khobragade et al.
Frontiers in bioengineering and biotechnology, 9, 757062-757062 (2021-10-26)
Herein, we report the development of a multi-enzyme cascade using transaminase (TA), esterase, aldehyde reductase (AHR), and formate dehydrogenase (FDH), using benzylamine as an amino donor to synthesize the industrially important compound sitagliptin intermediate. A panel of 16 TAs was
Marco Filice et al.
Nature protocols, 7(10), 1783-1796 (2012-09-08)
This protocol describes the regioselective deprotection of single hydroxyls in peracetylated monosaccharides and disaccharides by enzymatic or chemoenzymatic strategies. The introduction of a one-pot enzymatic step by using immobilized biocatalysts obviates the requirement to carry out tedious workups and time-consuming
Lipase
Pirahanchi Y and SharmaS
Biochemistry (2019)
Enzymatic synthesis of oligo- and polysaccharide fatty acid esters.
van den Broek, et al.
Carbohydrate Polymers, 93, 65-72 (2013)

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