62316
Lipase from Candida rugosa
powder, yellow-brown, ≥2 U/mg
Synonym(s):
CCL
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
biological source
fungus (Candida rugosa)
Quality Level
form
powder
specific activity
≥2 U/mg
mol wt
Mr ~67000
storage condition
dry at room temperature
concentration
≤100%
technique(s)
analytical sample preparation: suitable
color
yellow-brown
pH range
6.5—7.5 (0.01 g/L)
solubility
water: slightly soluble
application(s)
sample preservation
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
Gene Information
fungus ... LAP1(2544)
Looking for similar products? Visit Product Comparison Guide
General description
Research Area: Cell Signaling
The lipase enzyme is a naturally occurring enzyme present in both the stomach and pancreatic juice. It is expressed and active in various tissues. For instance, hepatic lipases are found in the liver, hormone-sensitive lipases in adipocytes, lipoprotein lipase on the vascular endothelial surface, and pancreatic lipase in the small intestine. These lipases are classified within the alpha/beta-hydrolase fold superfamily of enzymes.
The lipase enzyme is a naturally occurring enzyme present in both the stomach and pancreatic juice. It is expressed and active in various tissues. For instance, hepatic lipases are found in the liver, hormone-sensitive lipases in adipocytes, lipoprotein lipase on the vascular endothelial surface, and pancreatic lipase in the small intestine. These lipases are classified within the alpha/beta-hydrolase fold superfamily of enzymes.
Application
Lipase from Candida rugosa has been used to study and evaluate its effect on the anatomical structure and chemical composition of archaeological wood samples. It has also been used to remove the oily dirt from a child′s tunic dated to the Coptic period and also to study the effect of the enzymatic treatment on the mechanical and optical parameters of linen using scanning electron microscopy (SEM), Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), CIE-Lab values and ASTM method D5035.
Biochem/physiol Actions
Lipases, as a group of enzymes, are responsible for breaking down triglycerides into free fatty acids and glycerol, playing a pivotal role in the digestion, hydrolysis, and absorption of fat-soluble vitamins in pancreatic secretions. It contributes to the maintenance of proper gallbladder function. These enzymes, derived from animals, plants, and various microorganisms, are known for their stability and are often described as nature′s catalysts. While microbial lipases are the primary choice for commercial applications, they possess the unique ability to hydrolyze fats into fatty acids and glycerols at the water-lipid interface and can also reverse this reaction in non-aqueous environments. Elevated serum lipase levels can indicate pancreatitis. Understanding the role of lipase is essential for the pathophysiology of fat necrosis and acute and chronic pancreatitis. Lipases are also involved in the mechanism of some cholesterol-lowering medications.
Candida rugosa lipase is known to catalyze hydrolysis reactions, especially the production of ricinoleic acid.
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)
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Alexandra Kotogán et al.
Foods (Basel, Switzerland), 11(12) (2022-06-25)
Hydrolysis of olive, rapeseed, linseed, almond, peanut, grape seed and menhaden oils was performed with commercial lipases of Aspergillus niger, Rhizopus oryzae, Rhizopus niveus, Rhizomucor miehei and Candida rugosa. In chromogenic plate tests, olive, rapeseed, peanut and linseed oils degraded
Dominik Koszelewski et al.
Materials (Basel, Switzerland), 14(18) (2021-09-29)
A preliminary study of 2-amino-4-aryl-3,5-dicarbonitrile-6-thiopyridines as new potential antimicrobial drugs was performed. Special emphasis was placed on the selection of the structure of target pyridine derivatives with the highest biological activity against different types of Gram-stained bacteria by lipopolysaccharide (LPS).
Paweł Kowalczyk et al.
Materials (Basel, Switzerland), 15(5) (2022-03-11)
An enzymatic route for phosphorous-carbon- bond formation is developed by discovering new promiscuous activity of lipase. This biocatalytic transformation of phosphorous-carbon- bond addition leads to biologically and pharmacologically relevant α-acyloxy phosphonates with methyl group in α-position. A series of target
Hedwig Strohalm et al.
Journal of agricultural and food chemistry, 58(10), 6328-6333 (2010-04-27)
The preparation of ester enantiomers (acetates, butanoates, hexanoates and octanoates) of the secondary alcohols 2-pentanol, 2-heptanol and 2-nonanol via lipase-catalyzed kinetic resolutions was investigated. Conversion rates and stereochemical courses of esterification and hydrolysis reactions catalyzed by commercially available enzyme preparations
J Hall et al.
The Journal of small animal practice, 54(5), 275-279 (2013-02-13)
Mushroom toxicosis is rarely diagnosed in dogs and is poorly reported in the veterinary literature. This report suggests that mushroom toxicosis is a potentially under-diagnosed condition in first opinion practice in the UK. Nine dogs with clinical signs consistent with
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service