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Merck

L0777

Sigma-Aldrich

Lipase from Aspergillus oryzae

solution, ≥100,000 U/g, white, beige

Sinónimos:

AOL, Lipolase 100L

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About This Item

Número de CAS:
Comisión internacional de enzimas:
3.1.1.3.
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

origen biológico

Aspergillus sp. (Aspergillus oryzae)

formulario

solution

actividad específica

≥100,000 U/g

condiciones de almacenamiento

(Tightly closed. Dry)

técnicas

cell based assay: suitable

color

beige
white

Nº de acceso UniProt

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

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Descripción general

Research area: Cell Signaling

Lipase is derived from Aspergillus oryzae by ammonium sulfate precipitation and chromatography.Lipases or triacylglycerol acyl hydrolases are a group of hydrolase enzymes that are usually found in humans and animals with monogastric stomachs. Lipase enzymes are generally formed in the pancreas and stomach where they aid in fat and lipids digestion.(2)

Aplicación

Lipase from Aspergillus oryzae has been used:
  • as a control enzyme in activity assays
  • as a component in lipolase stock solution for the hydrolysis experiments
  • to incubate scaffolds for lipase-accelerated degradation experiments
  • as the lipolytic enzyme standard to detect lipolytic enzymatic activity via chromogenic agar plates and zymography

Acciones bioquímicas o fisiológicas

Lipase is widely used in several industries including food and pharmaceuticals. It mediates the hydrolysis of fats and oil. Lipase is utilized for peptide synthesis and in the detergent industry. It is active in the range of pH 2-5 and temperature between 30-50°C. Metal ions such as Fe2+, Fe3+, and Cu2+ prevent the action of lipase. A less polar organic solvent is preferred for high stability.Lipases play a crucial role in digestion as well as the transportation and processing of dietary lipid substrates by catalyzing the hydrolysis of ester bonds in lipid substrates. The lipase from Aspergillus oryzae (AOL), a multipurpose biocatalyst can be used in the kinetic resolution of a biotin intermediate lactone,α-lipoic acid, and 1-phenylethanol. Additionally, it has the ability to stereoselectively catalyze the hydrolysis of ethyl 2-(4-hydroxyphenoxy) propanoate and its analogs, which are key intermediates in the production of aryloxyphenoxypropionate herbicides. AOL serves as a promising biocatalyst in the esterification of a series of short-chain acids and alcohols to produce flavor esters. It can be used to catalyze the esterification of lauric acid with aromatic alcohol-benzyl alcohol.

Nota de preparación

Produced by submerged fermentation of a genetically modified Aspergillus oryzae microorganism

Información legal

A product of Novozyme Corp.

enzima

Referencia del producto
Descripción
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sustrato

Referencia del producto
Descripción
Precios

Pictogramas

Health hazard

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)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

E E van Haaften et al.
Acta biomaterialia, 92, 48-59 (2019-05-21)
To maintain functionality during in situ vascular regeneration, the rate of implant degradation should be closely balanced by neo-tissue formation. It is unknown, however, how the implant's functionality is affected by the degradation of the polymers it is composed of.
Microbial Enzyme in Food Biotechnology
Singh P and Kumar S
Enzymes in Food Biotechnology, 19-28 (2019)
E E van Haaften et al.
Acta biomaterialia, 92, 48-59 (2019-05-21)
To maintain functionality during in situ vascular regeneration, the rate of implant degradation should be closely balanced by neo-tissue formation. It is unknown, however, how the implant's functionality is affected by the degradation of the polymers it is composed of.
Lipolase catalyzed synthesis of benzyl esters of fatty acids
Shintre MS, et al.
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