L1754
Lipase from Candida rugosa
Type VII, ≥700 unit/mg solid
Synonym(s):
Triacylglycerol acylhydrolase, Triacylglycerol lipase
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About This Item
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biological source
fungus (candida rugosa)
type
Type VII
form
lyophilized
specific activity
≥700 unit/mg solid
storage condition
(Tightly closed. Dry)
technique(s)
cell based assay: suitable
color
beige
white
solubility
water: slightly soluble
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 Structure
Lipases are found in pancreatic secretions. This class of enzymes contains α and β hydrolase folds. Candida rugosa produces multiple lipase isoenzymes that have 80% sequence homology.
Lipases are found in pancreatic secretions. This class of enzymes contains α and β hydrolase folds. Candida rugosa produces multiple lipase isoenzymes that have 80% sequence homology.
Application
Lipase from Candida rugosa has been used:
- to synthesize dextran fatty acid esters
- to study the effect of lipase on conjugated linoleic acid (CLA1 and CLA2) production in the presence of sunflower oil and castor oil
- to prepare pH-imprinted enzyme for lipase-catalyzed transesterification of dextran T-40 with vinyl decanoate
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.
Biochem/physiol Actions
Lipases are enzymes and biocatalysts that catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids. They are useful for biotransformation reactions. It possesses broad substrate tolerance and is highly stereo- and regioselective. Lipases mediate lipid transport. Elevated levels of serum lipase are observed in pancreatitis. Lipases are the preferred catalysts for long-chain fatty acids. Lipases can be used in a wide range of solvents, in both aqueous and non-aqueous media, and thus have found use in applications like organic synthesis.
Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
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. (This is equivalent to approx. 10 microliters of CO2 in 30 minutes.)
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
Certificates of Analysis (COA)
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Marco Filice et al.
Nature protocols, 7(10), 1783-1796 (2012-09-08)
This protocol describes the regioselective deprotection of single hydroxyls in peracetylated monosaccharides and disaccharides by enzymatic or chemoenzymatic strategies. The introduction of a one-pot enzymatic step by using immobilized biocatalysts obviates the requirement to carry out tedious workups and time-consuming
Taresh P Khobragade et al.
Frontiers in bioengineering and biotechnology, 9, 757062-757062 (2021-10-26)
Herein, we report the development of a multi-enzyme cascade using transaminase (TA), esterase, aldehyde reductase (AHR), and formate dehydrogenase (FDH), using benzylamine as an amino donor to synthesize the industrially important compound sitagliptin intermediate. A panel of 16 TAs was
Kultida Kaewprapan et al.
Journal of bioscience and bioengineering, 112(2), 124-129 (2011-05-24)
Vinyl decanoate-modified dextran macromolecules (DexT40-VD) were synthesized in dimethyl sulfoxide at 50°C using lipase AY from Candida rugosa for catalyzing transesterification between polysaccharide and vinyl fatty esters. The extent of dextran modification (quantified by the molar ratio of attached alkyl
Lan Zhu et al.
Structure (London, England : 1993), 28(10), 1149-1159 (2020-08-01)
The lipidic cubic phase (LCP) technique has proved to facilitate the growth of high-quality crystals that are otherwise difficult to grow by other methods. However, the crystal size optimization process could be time and resource consuming, if it ever happens.
Yu-Cheng Lin et al.
The American journal of clinical nutrition, 99(4), 869-874 (2014-01-31)
A genome-wide association study identified variants in or near patatin-like phospholipase domain-containing-3 (PNPLA3), neurocan (NCAN), lysophospholipase-like 1 (LYPLAL1), glucokinase regulatory protein (GCKR), and protein phosphatase 1 regulatory subunit 3b (PPP1R3B) that were strongly associated with nonalcoholic fatty liver disease (NAFLD)
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