4-Nitrophenyl Palmitate
(Synonyms: 棕榈酸对硝基苯酯) 目录号 : GC46672
A colorimetric lipase and esterase substrate
Cas No.:1492-30-4
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
4-Nitrophenyl palmitate is a colorimetric lipase and esterase substrate.1 Upon enzymatic hydrolysis of 4-nitrophenyl palmitate, 4-nitrophenol is released which can be quantified by colorimetric detection at 410 nm as a measure of enzyme activity. 4-Nitrophenyl palmitate has been used to characterize the activity of various bacterial and mammalian enzymes, including Burkholderia and porcine pancreatic lipases.
1.Gupta, N., Rathi, P., and Gupta, R.Simplified para-nitrophenyl palmitate assay for lipases and esterasesAnal. Biochem.311(1)98-99(2002)
| Cas No. | 1492-30-4 | SDF | |
| 别名 | 棕榈酸对硝基苯酯 | ||
| Canonical SMILES | O=C(CCCCCCCCCCCCCCC)OC1=CC=C([N+]([O-])=O)C=C1 | ||
| 分子式 | C22H35NO4 | 分子量 | 377.5 |
| 溶解度 | DMF: 1 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 2.649 mL | 13.245 mL | 26.4901 mL |
| 5 mM | 0.5298 mL | 2.649 mL | 5.298 mL |
| 10 mM | 0.2649 mL | 1.3245 mL | 2.649 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Three-Dimensional Chiral Supramolecular Microenvironment Strategy for Enhanced Biocatalysis
ACS Nano 2021 Sep 28;15(9):14972-14984.PMID:34491712DOI:10.1021/acsnano.1c05212.
How the three-dimensional (3D) chiral environment affects the biocatalysis remains an important issue, thereby inspiring the development of a microenvironment that highly mimics the natural features of enzyme to guarantee enhanced biocatalysis. In this study, two gelators bearing d/l-phenylalanine as chiral centers are designed to construct the 3D chiral catalytic microenvironment for enhancing the biocatalysis of lipase. Such a microenvironment is programmed through chiral transmission of chirality from molecular chirality to achiral polymers. It shows that the chirality of the microenvironment evidently influences the catalytic efficiency of immobilized lipase inside the system, and the 3D microenvironment constructed by right-handed helical nanostructures can enhance the catalytic activity of lipase inside as high as 10-fold for catalyzing 4-Nitrophenyl Palmitate (NPP) to 4-nitrophenol (NP) and 1.4-fold for catalyzing lipids to triglycerides (TGs) in 3T3-L1 cells than that of the achiral microenvironment. Moreover, the 3D chiral microenvironment has the merits of good catalytic efficiency, high storage stability, and efficient recyclability. This strategy of designing a 3D chiral microenvironment suitable for biocatalysis will overcome the present limitations of enzymatic immobilization in traditional materials and enhance the understanding of biocatalysis.
Immobilization of Candida rugosa lipase on magnetized Dacron: kinetic study
Artif Cells Blood Substit Immobil Biotechnol 2007;35(2):221-35.PMID:17453706DOI:10.1080/10731190601188380.
Candida rugosa lipase has been covalently immobilized on ferromagnetic azide polyethyleneterepthalate (Dacron) with specific activity retention of 16% for 4-Nitrophenyl Palmitate and 24% for hydrolysis of triolein in hexane. The immobilized enzyme was more thermal stable than the soluble one, retaining 78.8% of the activity after 1 h at 60 degrees C. Also, this immobilized derivative was stable at the storage at 4 degrees C. It has been used 5 cycles for pNPP hydrolysis without loss of activity. Soluble and immobilized Candida rugosa lipase showed a Michaelian behavior for fatty acid 4-nitrophenyl esters and different apparent K(M) values: 0.110 mM and 0.124 mM (4-Nitrophenyl Palmitate - C16); 0.193 mM and 0.235 mM (4-nitrophenyl laurate - C12) and 0.206 mM and 0.119 mM (4-nitrophenyl butyrate - C4), respectively. The immobilized lipase was more efficient for catalyzing the hydrolysis of 4-nitrophenyl esters with short chain length fatty acid (4-NPB - C4) than soluble enzyme. The ferromagnetic Dacron-lipase derivative was able to catalyze the synthesis of triolein from glycerol and oleic acid with 50% of conversion after 72 h at 40 degrees C.
Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity
Int J Mol Sci 2022 Jan 23;23(3):1262.PMID:35163184DOI:10.3390/ijms23031262.
Esterases and lipases can process amphiphilic esters used as drugs and prodrugs and impact their pharmacokinetics and biodistribution. These hydrolases can also process ester components of drug delivery systems (DDSs), thus triggering DDSs destabilization with premature cargo release. In this study we tested and optimized assays that allowed us to quantify and compare individual esterase contributions to the degradation of substrates of increased lipophilicity and to establish limitations in terms of substrates that can be processed by a specific esterase/lipase. We have studied the impact of carbonic anhydrase; phospholipases A1, A2, C and D; lipoprotein lipase; and standard lipase on the hydrolysis of 4-nitrophenyl acetate, 4-Nitrophenyl Palmitate, DGGR and POPC liposomes, drawing structure-property relationships. We found that the enzymatic activity of these proteins was highly dependent on the lipophilicity of the substrate used to assess them, as expected. The activity observed for classical esterases was diminished when lipophilicity of the substrate increased, while activity observed for lipases generally increased, following the interfacial activation model, and was highly dependent on the type of lipase and its structure. The assays developed allowed us to determine the most sensitive methods for quantifying enzymatic activity against substrates of particular types and lipophilicity.
Enzymatic hydrolysis in an aqueous organic two-phase system using centrifugal partition chromatography
J Chromatogr A 2015 Apr 24;1391:72-9.PMID:25773726DOI:10.1016/j.chroma.2015.02.071.
Multi-phase reaction systems, mostly aqueous organic systems, are used in enzyme catalysis to convert hydrophobic substrates which are almost insoluble in aqueous media. In this study, a Centrifugal Partition Chromatograph is used as a compact device for enzymatic multi-phase reaction that combines efficient substrate supply to the aqueous phase and separation of both phases in one apparatus. A process design procedure to systematically select the aqueous and organic phase to achieve stable and efficient reaction rates and operation conditions in Centrifugal Partition Chromatography for efficient mixing and separation of the phases is presented. The procedure is applied to the hydrolysis of 4-Nitrophenyl Palmitate with a lipase derived from Candida rugosa. It was found that the hydrolysis rate of 4-Nitrophenyl Palmitate was two times higher in Centrifugal Partition Chromatography than in comparable stirred tank reactor experiments.
Surface Modification of Fe(3)O(4)@SiO(2) Magnetic Nanoparticles for Immobilization of Lipase
J Nanosci Nanotechnol 2017 Jan;17(1):370-6.PMID:29620837DOI:10.1166/jnn.2017.10964.
Magnetic Fe(3)O(4) nanoparticles were prepared through hydrothermal method and coated with silica on the surface to obtain Fe3O4@SiO2 core–shell nanoparticles. After modification with different functional groups including aldehyde, amine and diimide, the nanoparticles were used as carrier for covalent immobilization of lipase. The nanoparticles with aldehyde groups showed highest immobilization yield (52.8%) and efficiency (86.5%). And the immobilization conditions including pH, temperature and the concentration of enzyme were optimized. After immobilization, the K m of lipase was altered from 2.3 to 3.2 mM. The thermal stability and pH stability were enhanced by immobilization at the investigated conditions: pH 5.0–8.0 and temperature 30–70 °C. After 10 batches conversion of 4-Nitrophenyl Palmitate into p-Nitrophenol, the immobilized lipase retained over 75% of the original activity. Compared with the commercial lipase Novozym435, the immobilized lipase showed better stability and higher catalytic efficiency. These results demonstrate that the immobilized lipase on the modified Fe3O4@SiO2 magnetic nanoparticles has enhanced stability and reusability, which make lipase of potential interest in a number of industrial applications.