This product is not tested for solubility. For activity testing purposes, it is solubilized at 500 - 1000 units per mL in cold deionized water.
A similar product, L3294, Lipase from Thermus flavus, may be dissolved in 50 mM Tris-HCl, pH 8.0.
Note that this may yield a slightly hazy solution. The solution is expected to be stable for at least one month at 2–8 °C. This information may also be applied to L8525, Lipase from Candida rugosa.
L8525
Lipase from Candida rugosa
lyophilized powder, ≥40,000 units/mg protein
Synonym(s):
Triacylglycerol acylhydrolase, Triacylglycerol lipase
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€156.00
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€518.00
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-619-9
MDL number:
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Product Name
Lipase from Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
InChI key
QWZUIMCIEOCSJF-CHHCPSLASA-N
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-;
biological source
fungus (Candida rugosa)
form
lyophilized powder
specific activity
≥40,000 units/mg protein
composition
Protein, ≥4.0%
foreign activity
α-amylase ≤0.05 unit/mg solid
protease ≤0.001 units/mg solid
storage temp.
2-8°C
Quality Level
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1 of 4
This Item | 62302 | 62316 | 62285 |
|---|---|---|---|
| biological source fungus (Candida rugosa) | biological source fungus (Candida rugosa) | biological source fungus (Candida rugosa) | biological source - |
| specific activity ≥40,000 units/mg protein | specific activity 15-25 U/mg | specific activity ≥2 U/mg | specific activity ~50 U/mg |
| form lyophilized powder | form lyophilized solid, powder (fine) | form powder | form powder |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| foreign activity α-amylase ≤0.05 unit/mg solid, protease ≤0.001 units/mg solid | foreign activity - | foreign activity - | foreign activity - |
| Quality Level 200 | Quality Level 100 | Quality Level 100 | Quality Level 100 |
Analysis Note
Protein determined by biuret.
Application
Lipase from C. rugosa is used to catalyze the synthesis of flavor esters such as pentyl propanoate and butyl butanoate used in food enhancement. [1]
Lipase from Candida rugosa has been used in a study to assess the influence of phase segregation on enzyme hydrolytic activity. [2]
Lipase from Candida rugosa has been used:
- in the hydrolysis of loaded polycaprolactone–20% tricalcium phosphate (PCL–TCP) composites[3]
- in adsorption of proteins in emulsan/alginate beads and in enzyme assays[4]
- to catalyse methanolysis and hydrolysis reactions[5]
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.
Biochem/physiol Actions
Lipases are used in detergent, food, leather, pharmaceutical and diary industries.[6] It has several characteristics like substrate specificity, stereospecificity and regioselectivity. It also participates in various bioconversion reactions like, hydrolysis, esterification, acidolysis and aminolysis.[7]
Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).
Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
General description
Microbes of plant and animal basis mainly produce lipase enzyme. It can also be produced by marine organisms.[6]
Other Notes
One unit will hydrolyze 1.0 microequivalent of fatty acid from a triglyceride in 1 hr at pH 7.2 at 37 °C using olive oil (30 minute incubation).
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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An in vitro evaluation of PCL-TCP composites as delivery systems for platelet-rich plasma
Rai B, et al.
Journal of Controlled Release : Official Journal of the Controlled Release Society, 107(2), 330-342 (2005)
Daniele Zappi et al.
Talanta, 194, 26-31 (2019-01-06)
A newly modified electrode based on glassy carbon (GC) has been prepared and characterized electrochemically for application in electroanalytical chemistry. In particular, a GC screen-printed electrode (SPE) has been modified with nanostructures, namely multi-walled carbon nanotubes (MWCNTs), and TiO2 nanoparticles
Mariangela Bellusci et al.
Biomacromolecules, 13(3), 805-813 (2012-02-03)
Microbial lipase from Candida rugosa was immobilized by physical adsorption onto an ethylene-vinyl alcohol polymer (EVAL) functionalized with acyl chlorides. To evaluate the influence of the reagent chain-length on the amount and activity of immobilized lipase, three differently long aliphatic
Enzymatic transesterification monitored by an easy-to-use Fourier transform infrared spectroscopy method
Natalello A, et al.
Biotechnology Journal, 8(1), 133-138 (2013)
A M Brzozowski et al.
Nature, 351(6326), 491-494 (1991-06-06)
Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols. They have been classified as serine hydrolases owing to their inhibition by diethyl p-nitrophenyl phosphate. Lipase activity is greatly increased at the lipid-water interface, a phenomenon
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