62316
Lipase from Candida rugosa
powder, yellow-brown, ≥2 U/mg
Sinónimos:
CCL
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About This Item
Productos recomendados
origen biológico
fungus (Candida rugosa)
Nivel de calidad
Formulario
powder
actividad específica
≥2 U/mg
mol peso
Mr ~67000
condiciones de almacenamiento
dry at room temperature
concentración
≤100%
técnicas
analytical sample preparation: suitable
color
yellow-brown
intervalo de pH
6.5—7.5 (0.01 g/L)
solubilidad
water: slightly soluble
aplicaciones
sample preservation
temp. de almacenamiento
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-;
Clave InChI
QWZUIMCIEOCSJF-CHHCPSLASA-N
Información sobre el gen
fungus ... LAP1(2544)
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Descripción general
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.
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.
Aplicación
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.
Acciones bioquímicas o fisiológicas
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.
Definición de unidad
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)
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Resp. Sens. 1
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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Los clientes también vieron
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)
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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