52001
Lipase, immobilized on Immobead 150 from Rhizomucor miehei
≥300 U/g
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biological source
fungus (Rhizomucor miehei)
Quality Level
form
powder
specific activity
≥300 U/g
storage temp.
2-8°C
1 of 4
This Item | 90678 | 89444 | 54327 |
|---|---|---|---|
| specific activity ≥300 U/g | specific activity ≥600 U/g | specific activity ≥100 U/g | specific activity ≥900 U/g |
| biological source fungus (Rhizomucor miehei) | biological source Pseudomonas fluorescens | biological source - | biological source bacterial (Pseudomonas cepacia) |
| 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 |
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.[1]
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)
Storage Class
11 - Combustible Solids
wgk_germany
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
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