Skip to Content
MilliporeSigma
All Photos(2)

Documents

L8525

Sigma-Aldrich

Lipase from Candida rugosa

lyophilized powder, ≥40,000 units/mg protein

Synonym(s):

Triacylglycerol acylhydrolase, Triacylglycerol lipase

Sign Into View Organizational & Contract Pricing
All Photos(2)

About This Item

CAS Number:
9001-62-1
Enzyme Commission number:
3.1.1.3 (BRENDA, IUBMB)
EC Number:
232-619-9
MDL number:
MFCD00131509
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (Candida rugosa)

Quality Level

200

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

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

Looking for similar products? Visit Product Comparison Guide

General description

Microbes of plant and animal basis mainly produce lipase enzyme. It can also be produced by marine organisms.

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.
Lipase from Candida rugosa has been used in a study to assess the influence of phase segregation on enzyme hydrolytic activity.
Lipase from Candida rugosa has been used:
  • in the hydrolysis of loaded polycaprolactone–20% tricalcium phosphate (PCL–TCP) composites
  • in adsorption of proteins in emulsan/alginate beads and in enzyme assays
  • to catalyse methanolysis and hydrolysis reactions

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. It has several characteristics like substrate specificity, stereospecificity and regioselectivity. It also participates in various bioconversion reactions like, hydrolysis, esterification, acidolysis and aminolysis.
Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).

Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.

Unit Definition

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).

Analysis Note

Protein determined by biuret.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Customers Also Viewed

Slide 1 of 5

1 of 5

Lipase from Pseudomonas sp. Type XIII, lyophilized powder, ≥15 units/mg solid

Sigma-Aldrich

L9518

Lipase from Pseudomonas sp.

Lipase from Mucor miehei lyophilized powder, ≥4,000 units/mg solid (using olive oil)

Sigma-Aldrich

L9031

Lipase from Mucor miehei

Lipase from Rhizopus oryzae powder (fine), ~10 U/mg

Sigma-Aldrich

62305

Lipase from Rhizopus oryzae

Lipase from Candida sp. recombinant, expressed in Aspergillus niger

Sigma-Aldrich

L3170

Lipase from Candida sp.

Lipase from Rhizopus oryzae powder, light brown, ≥30 U/mg

Sigma-Aldrich

80612

Lipase from Rhizopus oryzae

Studies on the specificity of Candida rugosa lipase catalyzed esterification reactions in organic media.
BEZBRADICA, D.
J. Serb. Chem. Soc., 71, 31?41-31?41 (2006)
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
Triggered release of proteins from emulsan-alginate beads
Castro G R, et al.
Journal of Controlled Release : Official Journal of the Controlled Release Society, 109(1-3), 149-157 (2005)
Marine fungal and bacterial isolates for lipase production: A comparative study
Advances in Food and Nutrition Research, 78, 71-94 (2016)
Enzymatic transesterification monitored by an easy-to-use Fourier transform infrared spectroscopy method
Natalello A, et al.
Biotechnology Journal, 8(1), 133-138 (2013)
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service