L0777
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
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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
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)
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.
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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)
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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)
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Cech J, et al.
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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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