Tripropionin
Tripropionin structure
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Common Name | Tripropionin | ||
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| CAS Number | 139-45-7 | Molecular Weight | 260.28400 | |
| Density | 1.082 | Boiling Point | 175-176 °C20 mm Hg(lit.) | |
| Molecular Formula | C12H20O6 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | >230 °F | |
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Understanding the Mechanism of Enzyme-Induced Formation of Lyotropic Liquid Crystalline Nanoparticles.
Langmuir 31 , 6933-41, (2015) Liquid crystalline nanoparticles have shown great potential for application in fields of drug delivery and agriculture. However, optimized approaches to generating these dispersions have long been sought after. This study focused on understanding the mechanis... |
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Biochemical Characterization and Molecular Modeling of Pancreatic Lipase from a Cartilaginous Fish, the Common Stingray (Dasyatis pastinaca).
Appl. Biochem. Biotechnol. 176 , 151-69, (2015) In order to identify fish enzymes displaying novel biochemical properties, we have chosen the common stingray (Dasyatis pastinaca), one of the most primitive living jawed aquatic vertebrates as a starting biological material to purify a lipase. A stingray pan... |
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Enzymatic hydrolysis of organic-core microcapsules to produce aqueous-core microcapsules.
J. Microencapsul. 25(3) , 179-86, (2008) This paper describes the development of a new method to obtain aqueous-core microcapsules from organic-core capsules. The direct production of microcapsules, using tripropionin as organic material, followed by the hydrolysis of the core by a lipase was invest... |
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Lipase-catalysed hydrolysis of short-chain substrates in solution and in emulsion: a kinetic study.
Biochim. Biophys. Acta 1534(1) , 34-44, (2001) We have studied the enzymatic hydrolysis of solutions and emulsions of vinyl propionate, vinyl butyrate and tripropionin by lipases of various origin and specificity. Kinetic studies of the hydrolysis of short-chain substrates by microbial triacylglycerol lip... |
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Binding of human pancreatic carboxylic ester hydrolase to lipid interfaces.
Biochim. Biophys. Acta 659(2) , 401-10, (1981) Human pancreatic carboxylic ester hydrolase (EC 3.1.1.1), usually characterized by its activity on water-soluble substrates, is shown to catalyze reactions taking place at a lipid/water interface. The inhibition of tributyrin hydrolysis by 1-alcohols follows ... |
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Purification and characterization of a novel lipase from the digestive glands of a primitive animal: the scorpion.
Biochim. Biophys. Acta 1726(1) , 67-74, (2005) Higher animal's lipases are well characterized, however, much less is known about lipases from primitive ones. We choose the scorpion, one of the most ancient invertebrates, as a model of a primitive animal. A lipolytic activity was located in the scorpion di... |
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A newly high alkaline lipase: an ideal choice for application in detergent formulations.
Lipids Health Dis. 10 , 221, (2011) Bacterial lipases received much attention for their substrate specificity and their ability to function in extreme environments (pH, temperature...). Many staphylococci produced lipases which were released into the culture medium. Reports of thermostable lipa... |
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Distinction between esterases and lipases: a kinetic study with vinyl esters and TAG.
Lipids 37(7) , 653-62, (2002) The better to characterize enzymes hydrolyzing carboxyl ester bonds (carboxyl ester hydrolases), we have compared the kinetic behavior of various lipases and esterases against solutions and emulsions of vinyl esters and TAG. Short-chain vinyl esters are hydro... |
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Biochemical characterization, cloning, and molecular modelling of chicken pancreatic lipase.
Arch. Biochem. Biophys. 451(2) , 149-59, (2006) Chicken pancreatic lipase (CPL) was purified from delipidated pancreas. Pure CPL was obtained after ammonium sulphate fractionation, then DEAE-cellulose, Sephacryl S-200 gel filtration, and FPLC Mono-Q Sepharose columns. The pure lipase is a glycosylated mono... |
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Kinetic properties of Penicillium cyclopium lipases studied with vinyl esters.
Lipids 35(8) , 919-25, (2000) Penicillium cyclopium produces two lipases with different substrate specificities. Lipase I is predominantly active on triacylglycerols whereas lipase II hydrolyzes mono- and diacylglycerols but not triacylglycerols. In this study, we compared the kinetic pro... |