62302
Lipase from Candida rugosa
lyophilized, powder (fine), 15-25 U/mg
Synonym(s):
CCL
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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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.
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.
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.
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
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
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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
A. Gutman et al.
Tetrahedron, 48, 8775-8775 (1992)
Y. Ikushima et al.
Chemistry Letters (Jpn), 109-109 (1993)
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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