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Merck

62316

Sigma-Aldrich

Lipase aus Candida rugosa

powder, yellow-brown, ≥2 U/mg

Synonym(e):

CCL

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About This Item

CAS-Nummer:
EC-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

fungus (Candida rugosa)

Qualitätsniveau

Form

powder

Spezifische Aktivität

≥2 U/mg

Mol-Gew.

Mr ~67000

Lagerbedingungen

dry at room temperature

Konzentration

≤100%

Methode(n)

analytical sample preparation: suitable

Farbe

yellow-brown

pH-Bereich

6.5—7.5 (0.01 g/L)

Löslichkeit

water: slightly soluble

Anwendung(en)

sample preservation

Lagertemp.

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-;

InChIKey

QWZUIMCIEOCSJF-CHHCPSLASA-N

Angaben zum Gen

fungus ... LAP1(2544)

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Allgemeine Beschreibung

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.

Anwendung

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. Wirkung

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.

Einheitendefinition

1 U entspricht der Enzymmenge, die 1 μmol Ölsäure pro Minute bei pH 8.0 und 40°C freisetzt (Triolein, Fluka®-Nr. 62314 als Substrat)

Piktogramme

Health hazard

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Lipases: sources, production, purification, and applications
Patel N, et al.
Recent Patents on Biotechnology, 13(1), 45-56 (2019)
Biochemistry, lipase
Pirahanchi Y and Sharma S
StatPearls [Internet] (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)
Dominik Koszelewski et al.
Materials (Basel, Switzerland), 14(18) (2021-09-29)
A preliminary study of 2-amino-4-aryl-3,5-dicarbonitrile-6-thiopyridines as new potential antimicrobial drugs was performed. Special emphasis was placed on the selection of the structure of target pyridine derivatives with the highest biological activity against different types of Gram-stained bacteria by lipopolysaccharide (LPS).
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

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