An Anionic Surfactant Metallomicelle: Catalytic Activity and Mechanism for the Catalytic Hydrolysis of a Phosphate Ester

2014 ◽  
Vol 39 (3) ◽  
pp. 262-272 ◽  
Author(s):  
Lan Yu ◽  
Jia-qing Xie ◽  
Fan-zhen Li
2012 ◽  
Vol 554-556 ◽  
pp. 353-356
Author(s):  
Shu Lan Cai ◽  
Fa Mei Feng ◽  
Tao Wang ◽  
Xiu Lan Zhang

The catalytic hydrolysis of Bis(p-nitrophenyl) phosphate ester (BNPP) in the metallomicelle made up of Ce3+-diethylenetriamine and LSS (N-lauroyl sarcosinate) was investigated by UV/VIS method. The effect of the catalytic efficiency and stability of the system was studied under the different conditions. The results indicated that the catalytic system exhibited high activity, stability and reproducibility in the BNPP catalytic hydrolysis under proper proportion of Ce3+ion and diethylenetriamine, pH and temperature when the concentration of LSS is higher than its CMC (critical micelle concentration). The results also showed that the active species is the complex made up of Ce3+ion and diethylenetriamine.


RSC Advances ◽  
2017 ◽  
Vol 7 (64) ◽  
pp. 40354-40361 ◽  
Author(s):  
Kai Li ◽  
Xin Song ◽  
Guijian Zhang ◽  
Chi Wang ◽  
Ping Ning ◽  
...  

Fe/nano-AC has good catalytic activity for CS2 hydrolysis. The activity of the catalyst was affected by the amount of pores (5–10 nm). Metal species affected the oxidation of H2S. The solution pH and fluoride affected the generation of Fe3+.


Nanoscale ◽  
2018 ◽  
Vol 10 (45) ◽  
pp. 21466-21474 ◽  
Author(s):  
Hong Zhao ◽  
Guiqin Yu ◽  
Man Yuan ◽  
Jin Yang ◽  
Dan Xu ◽  
...  

Highly dispersed ultrafine Pt nanoparticles were confined in a triazinyl-containing porous organic polymer for the catalytic hydrolysis of ammonia borane and the selective hydrogenation of halogenated nitrobenzenes with excellent catalytic activity.


2012 ◽  
Vol 554-556 ◽  
pp. 345-348
Author(s):  
Min Wang ◽  
Li Qin Xu ◽  
Ci Li ◽  
Bing Ying Jiang ◽  
Jia Qing Xie

A macro-cyclic Schiff base ligand and the corresponding Cu (II) and Ni (II) complexes were synthesized and characterized. And the catalytic efficiency of the metallomicelles made of these complexes and noninonic micelle Brij35, as mimetic hydrolytic metalloenzyme, was investigated in the catalytic hydrolysis of bis(p-nitrophenyl) phosphate (BNPP) in this paper. The results show that the rate of the BNPP hydrolysis in the metallomicelles is about 106 -fold faster than that of the BNPP spontaneous hydrolysis in aqueous solution at the same conditions. The analysis of the characteristic absorption spectra of the hydrolytic reaction systems indicates that the key intermediate, composing of BNPP and Ni(II) or Cu(II) complexes, has been formed and the catalytic hydrolysis of BNPP is an intramolecular nucleophilic substitution reaction. Based on the results of characteristic absorption spectra, the mechanism of BNPP catalytic hydrolysis has been proposed and also the corresponding kinetic mathematical model has been established.


2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.


2019 ◽  
Vol 17 (1) ◽  
pp. 544-556
Author(s):  
Yoke-Leng Sim ◽  
Beljit Kaur

AbstractPhosphate ester hydrolysis is essential in signal transduction, energy storage and production, information storage and DNA repair. In this investigation, hydrolysis of adenosine monophosphate disodium salt (AMPNa2) was carried out in acidic, neutral and alkaline conditions of pH ranging between 0.30-12.71 at 60°C. The reaction was monitored spectrophotometrically. The rate ranged between (1.20 ± 0.10) × 10-7 s-1 to (4.44 ± 0.05) × 10-6 s-1 at [NaOH] from 0.0008 M to 1.00M recorded a second-order base-catalyzed rate constant, kOH as 4.32 × 10-6 M-1 s-1. In acidic conditions, the rate ranged between (1.32 ± 0.06) × 10-7 s-1 to (1.67 ± 0.10) × 10-6 s-1 at [HCl] from 0.01 M to 1.00 M. Second-order acid-catalyzed rate constant, kH obtained was 1.62 × 10-6 M-1 s-1. Rate of reaction for neutral region, k0 was obtained from graphical method to be 10-7 s-1. Mechanisms were proposed to involve P-O bond cleavage in basic medium while competition between P-O bond and N-glycosidic cleavage was observed in acidic medium. In conclusion, this study has provided comprehensive information on the kinetic parameters and mechanism of cleavage of AMPNa2 which mimicked natural AMP cleavage and the action of enzymes that facilitate its cleavage.


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