N0252
对硝基苯酚癸
lipase substrate, ≥98% (TLC), powder
别名:
4-硝基苯基癸酸酯, 癸酸4-硝基苯酯
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关于此项目
经验公式（希尔记法）:
C16H23NO4
化学文摘社编号:
分子量:
293.36
NACRES:
NA.83
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
Beilstein/REAXYS Number:
1915230
产品名称
对硝基苯酚癸, lipase substrate
InChI
1S/C16H23NO4/c1-2-3-4-5-6-7-8-9-16(18)21-15-12-10-14(11-13-15)17(19)20/h10-13H,2-9H2,1H3
SMILES string
CCCCCCCCCC(=O)Oc1ccc(cc1)[N+]([O-])=O
InChI key
RRNKCSIEGPOIKI-UHFFFAOYSA-N
assay
≥98% (TLC)
form
powder
solubility
chloroform: soluble 100 mg/mL, colorless to faintly yellow
storage temp.
−20°C
Quality Level
Application
癸酸 4-硝基苯酯可作为底物，以评估重组灰霉青霉 T55 菌株产生的羧酸酯酶。它也已用于肝胰腺提取物的一般酯酶活性测定。
癸酸 4-硝基苯酯已用作分光光度法评估脂肪酶活性的底物。它也已被用作估计羧酸酯酶活性的底物。
Biochem/physiol Actions
癸酸 4-硝基苯酯是脂肪酶的底物。与其他 4-硝基苯酯相比，胞外脂肪酶与 4-硝基苯基癸酸酯的水解反应速度更高。
Methods in Molecular biology: Platelets and Megakaryocytes, volume 1, functional assays, 27-27 (2012)
V M Gumerov et al.
Prikladnaia biokhimiia i mikrobiologiia, 48(4), 376-382 (2012-10-06)
As a result of sequencing the genome of the termophilic alkali-tolerant lipolytic bacterium Thermosyntropha lipolytica, the gene encoding a lipase secreted into the medium was identified. The recombinant enzyme was expressed in Escherichia coli. It was isolated, purified, and functionally
Janaina Marques de Almeida et al.
Scientific reports, 8(1), 10000-10000 (2018-07-04)
We determined the effect of the His-tag on the structure, activity, stability and immobilization of LipC12, a highly active lipase from a metagenomic library. We purified LipC12 with a N-terminal His-tag and then removed the tag using tobacco etch virus
Isolation and characterization of an enzyme from the Greenshell? mussel Perna canaliculus that hydrolyses pectenotoxins and esters of okadaic acid
MacKenzie LA, et al.
Toxicon, 60(3), 406-419 (2012)
Dan Wu et al.
Frontiers in bioengineering and biotechnology, 8, 844-844 (2020-08-28)
The multiple inhibitors tolerance of microorganism is important in bioconversion of lignocellulosic biomass which is a promising renewable and sustainable source for biofuels and other chemicals. The disruption of an unknown α/β hydrolase, which was termed KmYME and located in
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