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Sigma-Aldrich

Lipase from Candida rugosa

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

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Synonym(s):
CCL
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

fungus (Candida rugosa)

Quality Level

form

lyophilized solid
powder (fine)

quality

lyophilized

specific activity

15-25 U/mg

mol wt

Mr ~67000

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

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Application

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

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.

Unit Definition

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)

Other Notes

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

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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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
Y. Ikushima et al.
Chemistry Letters (Jpn), 109-109 (1993)
A. Gutman et al.
Tetrahedron, 48, 8775-8775 (1992)
K. Hult et al.
Indian J. Chem. B, 32, 123-123 (1993)
Guan-Chun Chen et al.
Biotechnology letters, 33(3), 525-529 (2010-11-04)
Triacylglycerol lipase from Pseudomonas cepacia and Fe(3)O(4) magnetic nanoparticles were encapsulated simultaneously within biomimetic silica through the catalysis of polyallylamine. The encapsulation efficiency reached 96% with an activity recovery of 51%. After 5 h at 37°C, the activities of the

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