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Merck

62302

Lipase from Candida rugosa

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

Synonym(s):

CCL

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-619-9
EC Number:
MDL number:
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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

Mr ~67000

storage temp.

2-8°C

Quality Level

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Application

Lipase from Candida rugosa has been used:
  • for the resolution of chiral compounds and the transesterification production of biodiesel.
  • for studying the immobilization of different lipase enzymes on graphene oxide support for high-efficiency biocatalysis.

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.

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.

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; Stereoselective ester synthesis; Benzyl-alkyl transesterification under mild neutral conditions; Enantioselectivity of some lipases: Review

pictograms

Health hazard

signalword

Danger

hcodes

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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Lipase enzymes on graphene oxide support for high-efficiency biocatalysis
Hermanova S, et al.
Applied Materials Today, 5, 200- 208 (2016)
A. Gutman et al.
Tetrahedron, 48, 8775-8775 (1992)
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)
Biochemistry, Lipase
Pirahanchi Y and Sharma S
StatPearls [Internet] (2023)

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