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L8906

Sigma-Aldrich

Lipase from Mucor javanicus

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

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Synonym(s):
Triacylglycerol acylhydrolase, Triacylglycerol lipase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

form

lyophilized powder

Quality Level

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 Information

常规特殊物品

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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)
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
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
C Guo et al.
Letters in applied microbiology, 55(6), 453-459 (2012-10-17)
This study aims to assess the removal mechanism of patulin using heat-treated Saccharomyces cerevisiae cells and identify the role of different cell wall components in the binding process. In order to understand the binding mechanism, viable cells, heat-treated cells, cell

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