62316

Lipase from Candida rugosa

powder, yellow-brown, ≥2 U/mg

• Synonyme(s) : CCL
• Numéro CAS: 9001-62-1
• UNSPSC Code: 12352204
• NACRES: NA.54
• EC Number: 232-619-9
• Numéro CE : 3.1.1.3 (BRENDA, IUBMB)
• MDL number: MFCD00131509
• Specific activity: ≥2 U/mg
• Biological source: (from Candida rugosa)
• Concentration: ≤100%

Propriétés

• Quality Segment: 100
• biological source: (from Candida rugosa)
• form: powder
• specific activity: ≥2 U/mg
• 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)

Description

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.

Other Notes

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)

Informations sur la sécurité

• pictograms: GHS08
• signalword: Danger
• hcodes: H334
• pcodes: P261 - P284 - P501
• Hazard Classifications: Resp. Sens. 1
• Classe de stockage: 11 - Combustible Solids
• flash_point_f: Not applicable
• flash_point_c: Not applicable
• ppe: Eyeshields, Gloves, type N95 (US)