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About This Item
Empirical Formula (Hill Notation):
C22H35NO4
CAS Number:
Molecular Weight:
377.52
NACRES:
NA.83
PubChem Substance ID:
UNSPSC Code:
12352204
EC Number:
216-084-9
MDL number:
Beilstein/REAXYS Number:
1891754
Product Name
4-Nitrophenyl palmitate, lipase substrate
InChI key
LVZSQWIWCANHPF-UHFFFAOYSA-N
InChI
1S/C22H35NO4/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-22(24)27-21-18-16-20(17-19-21)23(25)26/h16-19H,2-15H2,1H3
SMILES string
CCCCCCCCCCCCCCCC(=O)Oc1ccc(cc1)[N+]([O-])=O
assay
≥98% (TLC)
form
powder
solubility
chloroform: 100 mg/mL, clear, colorless to faintly yellow
storage temp.
−20°C
Quality Level
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Application
4-nitrophenyl palmitate has been used as a substrate for lipase enzyme activity.
General description
4-Nitrophenyl palmitate is a substrate for lipase enzyme activity. Lipase hydrolyzes 4-nitrophenyl palmitate and yields the yellow colored product 4-nitrophenol, which is measurable spectrophotometrically at 410 nm. This method is advantageous due to its short reaction time and facile spectrophotometric analyses. The cell-bound lipase has preference for 4-nitrophenyl palmitate as substrate than the extracellular lipase.
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Lipase and biosurfactant from Ochrobactrum intermedium strain MZV101 isolated by washing powder for detergent application
Zarinviarsagh M, et al.
Lipids in Health and Disease, 16(1), 177-177 (2017)
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Herein, as a promising support, a magnetic enzyme nanoformulation have been designed and fabricated by a poly-o-toluidine modification approach. Owing to the magnetic nature and the existence of amine functionalized groups, the as-synthesised poly(o-toluidine) functionalized magnetic nanocomposite (Fe3O4@POT) was employed
M M Maia et al.
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Lipase (Glycerol ester hydrolase EC 3.1.1.3.) from a Brazilian strain of Fusarium solani FSI has been investigated. The effect of different carbon sources and trace elements added to basal medium was observed with the aim of improving enzyme production. Lipase
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The construction and screening of metagenomic libraries constitute a valuable resource for obtaining novel biocatalysts. In this work, we present the construction of a metagenomic library in Escherichia coli using fosmid and microbial DNA directly isolated from forest topsoil and
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