4-NITROPHENYL CAPRYLATE
4-NITROPHENYL CAPRYLATE structure
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Common Name | 4-NITROPHENYL CAPRYLATE | ||
|---|---|---|---|---|
| CAS Number | 1956-10-1 | Molecular Weight | 265.30500 | |
| Density | 1.0950g/ml | Boiling Point | N/A | |
| Molecular Formula | C14H19NO4 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus.
Extremophiles 19 , 933-47, (2015) A haloalkaliphilic solvent-tolerant lipase was produced from Alkalibacillus salilacus within 48 h of growth in liquid medium. An overall 4.9-fold enhanced production was achieved over unoptimized media after medium optimization by statistical approaches. Plac... |
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Inhibition of Cancer Cell Proliferation and Antiradical Effects of Decoction, Hydroalcoholic Extract, and Principal Constituents of Hemidesmus indicus R. Br.
Phytother Res. 29 , 857-63, (2015) Indian Sarsaparilla (Hemidesmus indicus R. Br.) is widely used in Indian traditional medicine. In the present work, we explored the effects of decoction, traditional Ayurvedic preparation, and hydroalcoholic extract, a phytocomplex more traditionally studied ... |
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Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase.
Biochemistry 48(48) , 11496-504, (2009) In this study, to explore the plasticity of the alpha/beta-hydrolase fold family, we converted bromoperoxidase A2 (BPO-A2) from Streptomyces aureofaciens to a lipase by structure comparison with lipase A (LipA) from Bacillus subtilis. These two enzymes have s... |
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Interfacial reaction dynamics and acyl-enzyme mechanism for lipoprotein lipase-catalyzed hydrolysis of lipid p-nitrophenyl esters.
J. Biol. Chem. 261(26) , 12016-21, (1986) The fatty acyl (lipid) p-nitrophenyl esters p-nitrophenyl caprylate, p-nitrophenyl laurate and p-nitrophenyl palmitate that are incorporated at a few mol % into mixed micelles with Triton X-100 are substrates for bovine milk lipoprotein lipase. When the conce... |
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Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineering.
Protein Cell. 2(6) , 497-506, (2011) The inherent evolvability of promiscuous enzymes endows them with great potential to be artificially evolved for novel functions. Previously, we succeeded in transforming a promiscuous acylaminoacyl peptidase (apAAP) from the hyperthermophilic archaeon Aeropy... |
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Extracellular lipases from Bacillus subtilis: regulation of gene expression and enzyme activity by amino acid supply and external pH.
FEMS Microbiol. Lett. 225(2) , 319-24, (2003) Bacillus subtilis secretes two lipases LipA and LipB into the culture medium. Both enzyme genes were differentially expressed depending on the growth conditions as determined by activity assays and Western blotting in B. subtilis mutant strains lipA, lipB, an... |
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Enhancing thermostability of a Rhizomucor miehei lipase by engineering a disulfide bond and displaying on the yeast cell surface.
Appl. Microbiol. Biotechnol. 85(1) , 117-26, (2009) To increase the thermostability of Rhizomucor miehei lipase, the software Disulfide by Design was used to engineer a novel disulfide bond between residues 96 and 106, and the corresponding double cysteine mutants were constructed. The R. miehei lipase mutant ... |
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Multifunctionality of liver alcohol dehydrogenase: kinetic and mechanistic studies of esterase reaction.
Arch. Biochem. Biophys. 213(2) , 635-42, (1982)
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Gel catalysts that switch on and off.
Proc. Natl. Acad. Sci. U. S. A. 97(18) , 9861-4, (2000) We report development of a polymer gel with a catalytic activity that can be switched on and off when the solvent composition is changed. The gel consists of two species of monomers. The major component, N-isopropylacrylamide, makes the gel swell and shrink i... |
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Partial characterization of a lipase from gypsy moth (lymantria dispar L.) larval midgut.
Folia Biol. (Krakow.) 56(1-2) , 103-10, (2008) Lipase activity of the gypsy moth (Lymantria dispar L.) was studied by the spectrophotometric method using crude homogenate of fifth-instar larval midgut tissues as the enzyme source and p-nitrophenyl caprylate (pNPC) as substrate. A Km value of 0.310 mM and ... |