Lipase from Candida rugosa

Name: Lipase from <I>Candida rugosa</I>
Brand: SIGMA

lyophilized, powder (fine), 15-25 U/mg

Synonym(s):

CCL

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About This Item

CAS Number:

9001-62-1

UNSPSC Code:

12352204

NACRES:

NA.54

EC Number:

232-619-9

EC Number:

3.1.1.3 (BRENDA, IUBMB)

MDL number:

MFCD00131509

Key Documents

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Product Name

Lipase from Candida rugosa, lyophilized, powder (fine), 15-25 U/mg

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 solid
powder (fine)

quality

lyophilized

specific activity

15-25 U/mg

mol wt

M_r ~67000

storage temp.

2-8°C

Quality Level

100

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Show Differences

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This Item	L8525	L1754	62285
Sigma-Aldrich 62302 Lipase from Candida rugosa	Sigma-Aldrich L8525 Lipase from Candida rugosa	Sigma-Aldrich L1754 Lipase from Candida rugosa	Sigma-Aldrich 62285 Lipase from Aspergillus oryzae
biological source fungus (Candida rugosa)	biological source fungus (Candida rugosa)	biological source fungus (candida rugosa)	biological source -
specific activity 15-25 U/mg	specific activity ≥40,000 units/mg protein	specific activity ≥700 unit/mg solid	specific activity ~50 U/mg
form lyophilized solid, powder (fine)	form lyophilized powder	form lyophilized	form powder
mol wt M_r ~67000	mol wt -	mol wt -	mol wt -
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 200	Quality Level 200	Quality Level 100

Application

Lipase from Candida rugosa has been used:

for the resolution of chiral compounds and the transesterification production of biodiesel.[1]
for studying the immobilization of different lipase enzymes on graphene oxide support for high-efficiency biocatalysis.[2]

Biochem/physiol Actions

Candida rugosa lipase is known to catalyze hydrolysis reactions, especially the production of ricinoleic acid.

Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.[3]

General description

Research area: Cell signaling

Lipase is a part of the alpha/beta-hydrolase fold superfamily of enzymes and is expressed in multiple tissues, including the liver, adipocytes, small intestine, and endothelial surface.[4]

Other Notes

1 U corresponds to the amount of enzyme which liberates 1 μmol oleic acid per minute at pH 8.0 and 40 °C (triolein, Cat. No. 62314 as substrate)

A highly stereospecific catalyst suitable for preparative resolution of racemic acids and alcohols[5]; Stereoselective ester synthesis[6]; Benzyl-alkyl transesterification under mild neutral conditions[7]; Enantioselectivity of some lipases: Review[8]

pictograms

GHS08

signalword

Danger

hcodes

H334

pcodes

P261 - P284 - P501

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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K. Hult et al.

Indian J. Chem. B, 32, 123-123 (1993)

A. Gutman et al.

Tetrahedron, 48, 8775-8775 (1992)

Lipase enzymes on graphene oxide support for high-efficiency biocatalysis

Hermanova S, et al.

Applied Materials Today, 5, 200- 208 (2016)

Y. Ikushima et al.

Chemistry Letters (Jpn), 109-109 (1993)

Comparison of different strategies for the lipase-catalyzed preparative resolution of racemic acids and alcohols: Asymmetric hydrolysis, esterification, and transesterification.

B Cambou et al.

Biotechnology and bioengineering, 26(12), 1449-1454 (1984-12-01)

Lipase from Candida cylindracea has been found to be a highly stereospecific catalyst suitable for preparative resolution of racemic acids and alcohols. Using (R, S)-2-(p-chlorophenoxy) propionic acid (whose R isomer is a herbicide) and (R, S)-sec-butanol (a versatile synthon) as

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