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L0777

Sigma-Aldrich

Lipase from Aspergillus oryzae

solution, ≥100,000 U/g, white, beige

Synonym(s):

AOL, Lipolase 100L

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About This Item

CAS Number:
Enzyme Commission number:
3.1.1.3.
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Aspergillus sp. (Aspergillus oryzae)

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

Product No.
Description
Pricing

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
Lipolase catalyzed synthesis of benzyl esters of fatty acids
Shintre MS, et al.
Biochemical Engineering Journal, 12, 131-141 (2002)
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.
Hong De Yan et al.
3 Biotech, 9(7), 265-265 (2019-06-21)
The lipase from Aspergillus oryzae was modified with a surfactant and then observed to exhibit high catalytic efficiency and enantioselectivity for the kinetic resolution of (RS)-1-phenylethanol. The influential factors of the modified-lipase preparation were investigated, including the surfactant source, the

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