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Merck

L0777

Sigma-Aldrich

Lipase aus Aspergillus oryzae

solution, ≥100,000 U/g, white, beige

Synonym(e):

AOL, Lipolase 100L

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About This Item

CAS-Nummer:
EC-Nummer:
3.1.1.3.
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

Aspergillus sp. (Aspergillus oryzae)

Qualitätsniveau

Form

solution

Spezifische Aktivität

≥100,000 U/g

Lagerbedingungen

(Tightly closed. Dry)

Methode(n)

cell based assay: suitable

Farbe

beige
white

UniProt-Hinterlegungsnummer

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

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Allgemeine Beschreibung

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)

Anwendung

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. Wirkung

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.

Angaben zur Herstellung

Produced by submerged fermentation of a genetically modified Aspergillus oryzae microorganism

Rechtliche Hinweise

Ein Produkt der Novozyme Corp.

Enzym

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Substrat

Produkt-Nr.
Beschreibung
Preisangaben

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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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.
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.
Three-phase slug flow in microchips can provide beneficial reaction conditions for enzyme liquid-liquid reactions
Cech J, et al.
Biomicrofluidics, 7(5), 054103-054103 (2013)
Dzhuliya Dzhonova et al.
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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