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Key Documents

62316

Sigma-Aldrich

Lipase from Candida rugosa

powder, yellow-brown, ≥2 U/mg

Synonym(s):

CCL

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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)

Quality Level

form

powder

specific activity

≥2 U/mg

mol wt

Mr ~67000

storage condition

dry at room temperature

concentration

≤100%

technique(s)

analytical sample preparation: suitable

color

yellow-brown

pH range

6.5—7.5 (0.01 g/L)

solubility

water: slightly soluble

application(s)

sample preservation

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

Gene Information

fungus ... LAP1(2544)

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General description

Research Area: Cell Signaling
The lipase enzyme is a naturally occurring enzyme present in both the stomach and pancreatic juice. It is expressed and active in various tissues. For instance, hepatic lipases are found in the liver, hormone-sensitive lipases in adipocytes, lipoprotein lipase on the vascular endothelial surface, and pancreatic lipase in the small intestine. These lipases are classified within the alpha/beta-hydrolase fold superfamily of enzymes.

Application

Lipase from Candida rugosa has been used to study and evaluate its effect on the anatomical structure and chemical composition of archaeological wood samples. It has also been used to remove the oily dirt from a child′s tunic dated to the Coptic period and also to study the effect of the enzymatic treatment on the mechanical and optical parameters of linen using scanning electron microscopy (SEM), Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), CIE-Lab values and ASTM method D5035.

Biochem/physiol Actions

Lipases, as a group of enzymes, are responsible for breaking down triglycerides into free fatty acids and glycerol, playing a pivotal role in the digestion, hydrolysis, and absorption of fat-soluble vitamins in pancreatic secretions. It contributes to the maintenance of proper gallbladder function. These enzymes, derived from animals, plants, and various microorganisms, are known for their stability and are often described as nature′s catalysts. While microbial lipases are the primary choice for commercial applications, they possess the unique ability to hydrolyze fats into fatty acids and glycerols at the water-lipid interface and can also reverse this reaction in non-aqueous environments. Elevated serum lipase levels can indicate pancreatitis. Understanding the role of lipase is essential for the pathophysiology of fat necrosis and acute and chronic pancreatitis. Lipases are also involved in the mechanism of some cholesterol-lowering medications.
Candida rugosa lipase is known to catalyze hydrolysis reactions, especially the production of ricinoleic acid.

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol oleic acid per minute at pH 8.0 and 40 °C (triolein, Cat. No. 62314 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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Lipases: sources, production, purification, and applications
Patel N, et al.
Recent Patents on Biotechnology, 13(1), 45-56 (2019)
Enzymatic removal of the oily dirt from a Coptic tunic using the enzyme lipase
Ahmed HE, et al.
The Journal of biological chemistry, 6(3) (2010)
Biochemistry, lipase
Pirahanchi Y and Sharma S
StatPearls [Internet] (2019)
Paweł Kowalczyk et al.
Materials (Basel, Switzerland), 15(5) (2022-03-11)
An enzymatic route for phosphorous-carbon- bond formation is developed by discovering new promiscuous activity of lipase. This biocatalytic transformation of phosphorous-carbon- bond addition leads to biologically and pharmacologically relevant α-acyloxy phosphonates with methyl group in α-position. A series of target
Alexandra Kotogán et al.
Foods (Basel, Switzerland), 11(12) (2022-06-25)
Hydrolysis of olive, rapeseed, linseed, almond, peanut, grape seed and menhaden oils was performed with commercial lipases of Aspergillus niger, Rhizopus oryzae, Rhizopus niveus, Rhizomucor miehei and Candida rugosa. In chromogenic plate tests, olive, rapeseed, peanut and linseed oils degraded

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