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L8906

Sigma-Aldrich

Lipase from Mucor javanicus

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

Synonyme(s) :

Triacylglycerol acylhydrolase, Triacylglycerol lipase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

lyophilized powder

Activité spécifique

≥300 units/mg solid (using olive oil)

Température de stockage

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-;

Clé InChI

QWZUIMCIEOCSJF-CHHCPSLASA-N

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Description générale

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.

Actions biochimiques/physiologiques

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

Définition de l'unité

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).

Remarque sur l'analyse

Protein determined by biuret.

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Screening and selection of lipases for the enzymatic production of polyglycerol polyricinoleate.
Bo?dalo, A.
Biochemical Engineering Journal, 46, 217-222 (2009)
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
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
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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