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52001

Lipase, immobilized on Immobead 150 from Rhizomucor miehei

≥300 U/g

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About This Item

NACRES:
NA.54
UNSPSC Code:
12352204
Specific activity:
≥300 U/g
Biological source:
fungus (Rhizomucor miehei)
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biological source

fungus (Rhizomucor miehei)

Quality Level

form

powder

specific activity

≥300 U/g

storage temp.

2-8°C

Application

Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Biochem/physiol Actions

Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
The lipase cleaves ester bonds of triacylglycerols with the subsequent release of free fatty acids, diacylglycerols, monoacylglycerols and glycerol. It can also catalyze the reverse reactions when the aqueous medium is replaced by an organic or a biphasic aqueous/organic medium.

Other Notes

1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 7.5 and 40°C (tributyrin, Cat. No. 91010, as substrate)

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This Item
906788944454327
biological source

fungus (Rhizomucor miehei)

biological source

Pseudomonas fluorescens

biological source

-

biological source

bacterial (Pseudomonas cepacia)

specific activity

≥300 U/g

specific activity

≥600 U/g

specific activity

≥100 U/g

specific activity

≥900 U/g

form

powder

form

powder

form

powder (or beads)

form

powder (or beads)

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100


Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Study of PLA pre-treatment, enzymatic and model-compost degradation, and valorization of degradation products to bacterial nanocellulose.
Sourkouni, et al.
World Journal of Microbiology & Biotechnology, 39, 161-161 (2023)
Kinetic studies on the Rhizomucor miehei lipase catalyzed esterification reaction of oleic acid with 1-butanol in a biphasic system
G.N. Kraai et al.
Biochem. Bioeng., 41, 87-94 (2008)
Ina Schoenfeld et al.
Biotechnology and bioengineering, 110(9), 2333-2342 (2013-03-28)
The use of enzymes as biocatalysts in organic media is an important issue in modern white biotechnology. However, their low activity and stability in those media often limits their full-scale application. Amphiphilic polymer conetworks (APCNs) have been shown to greatly



Global Trade Item Number

SKUGTIN
52001-50G04061832754246
52001-10G04061832546810

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