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MilliporeSigma

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.
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Aspergillus sp. (Aspergillus oryzae)

Quality Level

form

solution

specific activity

≥100,000 U/g

storage condition

(Tightly closed. Dry)

technique(s)

cell based assay: suitable

color

beige
white

UniProt accession no.

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

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General description

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)

Application

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

Biochem/physiol Actions

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.

Preparation Note

Produced by submerged fermentation of a genetically modified Aspergillus oryzae microorganism

Legal Information

A product of Novozyme Corp.

Enzyme

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Descripción
Precios

substrate

Referencia del producto
Descripción
Precios

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Purification and characterization of lipase produced by Aspergillus oryzae CJLU-31 isolated from waste cooking oily soil
Zhou J, et al.
American Journal of Food Technology, 7(10), 596-608 (2012)
E E van Haaften et al.
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Cech J, et al.
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PloS one, 13(8), e0203409-e0203409 (2018-08-31)
Local drug delivery systems that adjust the release of immunosuppressive drug in response to the nature and intensity of inflammation represent a promising approach to reduce systemic immunosuppression and its side effects in allotransplantation. Here we aimed to demonstrate that
Jing Li et al.
Materials today. Communications, 24, 101197-101197 (2020-08-25)
The low cost lipase derived from Thermomyces lanugionous was chosen to conjugate with Fe3O4 nanoparitcles as a magnetic responsive lipase (MRL) biocatalyst. The structure of MRL was observed by atomic force microscopy (AFM). The Fourier transform infrared (FTIR) spectroscopy analysis

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