54327
Lipase, immobilized on Immobead 150 from Pseudomonas cepacia
≥900 U/g
Synonym(s):
Immobilized Lipase
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
biological source
bacterial (Pseudomonas cepacia)
form
powder (or beads)
specific activity
≥900 U/g
color
white to off-white
application(s)
life science and biopharma
storage temp.
2-8°C
Gene Information
Burkholderia spp. ... BURCE16_RS29975(56665765)
General description
Research area: Cell Signaling
Lipases are water-soluble, ester hydrolases. Long aliphatic chain acyl esters of cholesterol (cholesteryl esters), triacyl esters of glycerol (triacylglycerols), acyl esters of long chain alcohols (wax esters), diacyl esters of glycerol (diacylglycerols), and monoacyl esters of glycerol, are some of the common substrates for lipases.
Lipases are water-soluble, ester hydrolases. Long aliphatic chain acyl esters of cholesterol (cholesteryl esters), triacyl esters of glycerol (triacylglycerols), acyl esters of long chain alcohols (wax esters), diacyl esters of glycerol (diacylglycerols), and monoacyl esters of glycerol, are some of the common substrates for lipases.
Application
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.Lipase, immobilized on Immobead 150 from Pseudomonas cepacia has been used in enzymatic hydrolysis of polylactic acid (PLA). It has also been used as biocatalysts in lipase-catalyzed kinetic resolution reactions.
Biochem/physiol Actions
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.Lipases are known to regulate energy metabolism of the cell. Lipolysis is highly essential for cellular uptake or release of fatty acids (FAs) and glycerol. Gastrointestinal lipolysis catabolizes dietary fat. Vascular lipolysis hydrolyzes lipoprotein-related triglycerides (LTPs) in the blood. In the intracellular domain, lipolysis catalyzes the breakdown of triglycerides (TGs) stored in LDLs for exportation of fatty acids (fat) (fat tissue) or metabolism (non-adipose tissue).
Unit Definition
1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 7.5 and 40°C (tributyrin, Cat. No. 91010, as substrate)
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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
Studies on the chemoenzymatic synthesis of (R)-and (S)-methyl 3-aryl-3-hydroxypropionates: the influence of toluene-pretreatment of lipase preparations on enantioselective transesterifications
Tetrahedron Asymmetry (2013)
ACS omega, 6(43), 29192-29200 (2021-11-09)
Deracemizations are clearly preferable to kinetic resolutions in the production of chiral molecules from racemates, as they allow up to 100% chemical and optical yield. Here we present a new process route for multienzymatic deracemizations that is relevant for reaction
Fatty Acid Signaling: The New Function of Intracellular Lipases
International Journal of Molecular Sciences, 3831?3855-3831?3855 (2015)
Cell metabolism, 15(3), 279-291 (2012-03-13)
Lipolysis is defined as the catabolism of triacylglycerols stored in cellular lipid droplets. Recent discoveries of essential lipolytic enzymes and characterization of numerous regulatory proteins and mechanisms have fundamentally changed our perception of lipolysis and its impact on cellular metabolism.
Lipases
Encyclopedia of Biological Chemistry, 729-732 (2013)
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