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Safety Information

L8906

Sigma-Aldrich

Lipase from Mucor javanicus

lyophilized powder, ≥300 units/mg solid (using olive oil)

Synonym(s):

Triacylglycerol acylhydrolase, Triacylglycerol lipase

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About This Item

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

form

lyophilized powder

specific activity

≥300 units/mg solid (using olive oil)

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

Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols.

Application

Lipase from Mucor javanicus can be used to catalyze the production of polyglycerol polyricinoleate from polyricinoleic acid and polyglycerol-3.
Lipase from Mucor javanicus has been used in a study to assess the effects of lyophilization time and water content on the salt-induced activation of enzymes in organic solvents.

Biochem/physiol Actions

Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).

Unit Definition

One unit will hydrolyze 1.0 microequivalent of fatty acid from a triglyceride in 1 hr at pH 7.7 at 37 °C using olive oil (30 minute incubation).

Analysis Note

Protein determined by biuret.

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

L8906-5G:
L8906-BULK:
L8906-1G:
L8906-VAR:


Certificates of Analysis (COA)

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Screening and selection of lipases for the enzymatic production of polyglycerol polyricinoleate.
Bo?dalo, A.
Biochemical Engineering Journal, 46, 217-222 (2009)
M T Ru et al.
Biotechnology and bioengineering, 63(2), 233-241 (1999-04-01)
The addition of simple inorganic salts to aqueous enzyme solutions prior to lyophilization results in a dramatic activation of the dried powder in organic media relative to enzyme with no added salt. Activation of both the serine protease subtilisin Carlsberg
Hani El-Nezami et al.
Journal of agricultural and food chemistry, 52(14), 4577-4581 (2004-07-09)
Viable, heat-and acid-killed Lactobacillus rhamnosus strain GG (LGG) has shown high binding properties with zearalenone (ZEN). To identify the type of chemical moieties and interactions involved in binding with the ZEN, LGG was subjected to different chemical and enzymatical treatments
A M Stepan et al.
Journal of biotechnology, 167(1), 16-23 (2013-06-19)
This is the first report on successful enzyme catalyzed surface esterification of hemicellulose films. Enzyme catalyzed surface acetylation with vinyl acetate and stearation with vinyl stearate were studied on rye arabinoxylan (AX) films. Different surface analytical techniques (FT-IR, TOF-SIMS, ESCA
Hidehiko Wakabayashi et al.
Journal of agricultural and food chemistry, 51(15), 4349-4355 (2003-07-10)
The enantioselectivity of the generation of 3-mercaptohexanal and 3-mercaptohexanol, two potent sulfur-containing aroma compounds, by lipase-catalyzed hydrolysis of the corresponding 3-acetylthioesters was investigated. The stereochemical course of the kinetic resolutions was followed by capillary gas chromatography using modified cyclodextrins as

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