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L9031

Sigma-Aldrich

Lipase from Mucor miehei

lyophilized powder, ≥4,000 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

≥4,000 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

Lipase is produced by several animals, microbes, and plants. Lipase from Mucor sp. is a fungal lipase. It is a member of the serine hydrolase family.

Application

Lipase from Mucor miehei can be used to drive the synthesis of flavor esters.
Lipase from Mucor miehei has been used in a study to assess the nonthermal effect of microwave irradiation in nonaqueous enzymatic esterification. It has also been used in a study to investigate the hydrolysis of virgin coconut oil using immobilized lipase in a batch reactor.
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Biochem/physiol Actions

Mucor miehei lipase hydrolizes triglycerides and catalyzes the synthesis of esters from glycerol and long-chain fatty acids in vitro. Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).
Microbial lipase has a wide industrial application due to its stability, broad substrate specificity, and selectivity. It may be used in the synthesis of biosurfactants and finds application in organic chemical processing, dairy industry, oleochemical industry, detergent formulations, paper, cosmetics, nutrition, and the pharmaceutical industry.

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.

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

L9031-500MG:
L9031-100MG:
L9031-VAR:
L9031-BULK:


Certificates of Analysis (COA)

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Lee Suan Chua et al.
Enzyme research, 2012, 542589-542589 (2012-09-07)
Hydrolysis of virgin coconut oil (VCO) had been carried out by using an immobilised lipase from Mucor miehei (Lipozyme) in a water-jacketed batch reactor. The kinetic of the hydrolysis was investigated by varying the parameters such as VCO concentration, enzyme
Design and synthesis of an affinity probe that targets caspases in proteomic experiments
Liau, M-L, et al
Tetrahedron Letters, 44, 1043-1046 (2003)
R Sharma et al.
Biotechnology advances, 19(8), 627-662 (2003-10-11)
Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) catalyze the hydrolysis and the synthesis of esters formed from glycerol and long-chain fatty acids. Lipases occur widely in nature, but only microbial lipases are commercially significant. The many applications of lipases include speciality organic
Agnieszka Stobiecka
Journal of photochemistry and photobiology. B, Biology, 80(1), 9-18 (2005-06-21)
Steady-state and time-resolved fluorescence-quenching measurements have been performed to study multitryptophan lipase from filamentous fungus Rhizomucor miehei. Using the steady-state acrylamide fluorescence quenching data and the fluorescence-quenching-resolved-spectra (FQRS) method, the total emission spectrum of native ("closed-lid") lipase has been decomposed
H S Ryu et al.
Applied microbiology and biotechnology, 70(3), 321-326 (2005-08-10)
A Photobacterium strain, M37, showing lipolytic activity, was previously isolated from an intertidal flat of the Yellow Sea in Korea and identified as Photobacterium lipolyticum sp. nov. In the present study, the corresponding gene was cloned using the shotgun method.

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