Effect of a double-structured microporous polymer support on the catalytic activity, stability and aggregation behavior of immobilized enzymes

2015 ◽  
Vol 64 (7) ◽  
pp. 915-923
Author(s):  
Haijie Yang ◽  
Lei Wang ◽  
Shuli Chen ◽  
Mian Wang ◽  
Zhiwei Feng
Keyword(s):  
Catalytic Activity ◽  
Immobilized Enzymes ◽  
Aggregation Behavior ◽  
Polymer Support ◽  
Microporous Polymer

Characterization and Catalytic Activity of Poly(4-Vinylpyridine-Co-Divinylbenzene)-Co2+ Complex

2005 ◽  
Vol 494 ◽  
pp. 363-368 ◽  
Author(s):  
D. Lončarević ◽  
Ž. Čupić
Keyword(s):  
Catalytic Activity ◽  
Molecular Level ◽  
Supported Catalysts ◽  
Lone Pair ◽  
Polymer Support ◽  
Polymeric Complex ◽  
Reaction Conditions ◽  
Pyridine Nitrogen ◽  
Nitrogen Lone Pair ◽  
Thermal Stability Of

Poly(4-vinylpyridine-co-divinylbenzene)-Co2+ was characterized using infrared spectroscopy (IR), thermogravimetric analysis (TG-DTA), N2-physisorption and polarography. Thermal analysis suggests sufficient thermal stability of the polymer support, under reaction conditions. From polarography measurements, the Co2+ content on polymer-supported catalysts is estimated and it was proved that no significant leaching occurred during the activity tests. At the molecular level, FTIR of P4VP-DVB-Co2+ reveals that the pyridine nitrogen lone pair coordinates to the metal center in the polymeric complex. The obtained P4VP-DVB-Co2+ catalysts performed interesting catalytic activity in reaction of the cyclohexane oxidation with air, indicating that increasing Co2+ content lowers the initiation temperature and raises the decomposition of cyclohexylhydroperoxide.

Hairy Particles with Immobilized Enzymes: Impact of Particle Topology on the Catalytic Activity

2018 ◽  
Vol 11 (1) ◽  
pp. 1645-1654 ◽  
Author(s):  
Claudia Marschelke ◽  
Martin Müller ◽  
Dorina Köpke ◽  
Anke Matura ◽  
Marco Sallat ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Immobilized Enzymes

scholarly journals Synthesis, Aggregation Behavior, and Catalytic Activity in the Ullmann Reaction of Amphiphilic p-tert-Butylthiacalix[4]arene with Azidoalkylimidazolium Moieties

2019 ◽  
Vol 12 (4) ◽  
pp. 340-345
Author(s):  
V. A. Burilov ◽  
R. I. Garipova ◽  
E. D. Sultanova ◽  
D. A. Mironova ◽  
V. G. Evtugyn ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Aggregation Behavior ◽  
Ullmann Reaction

scholarly journals Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine

Materials ◽  
2020 ◽  
Vol 13 (7) ◽  
pp. 1776 ◽  
Author(s):  
Massimiliano Magro ◽  
Davide Baratella ◽  
Andrea Venerando ◽  
Giulia Nalotto ◽  
Caroline R. Basso ◽  
...  
Keyword(s):  
Biological Activity ◽  
Catalytic Activity ◽  
Enzyme Immobilization ◽  
Self Assembly ◽  
Immobilized Enzymes ◽  
Biological Properties ◽  
Oxide Nanoparticles ◽  
Electrochemical Studies ◽  
Maghemite Nanoparticles ◽  
Surface Active

Generally, enzyme immobilization on nanoparticles leads to nano-conjugates presenting partially preserved, or even absent, biological properties. Notwithstanding, recent research demonstrated that the coupling to nanomaterials can improve the activity of immobilized enzymes. Herein, xanthine oxidase (XO) was immobilized by self-assembly on peculiar naked iron oxide nanoparticles (surface active maghemite nanoparticles, SAMNs). The catalytic activity of the nanostructured conjugate (SAMN@XO) was assessed by optical spectroscopy and compared to the parent enzyme. SAMN@XO revealed improved catalytic features with respect to the parent enzyme and was applied for the electrochemical studies of xanthine. The present example supports the nascent knowledge concerning protein conjugation to nanoparticle as a means for the modulation of biological activity.

Catalytic Activity in Organic Solvents and Stability of Immobilized Enzymes Depend on the Pore Size and Surface Characteristics of Mesoporous Silica

2000 ◽  
Vol 12 (11) ◽  
pp. 3301-3305 ◽  
Author(s):  
Haruo Takahashi ◽  
Bo Li ◽  
Toshiya Sasaki ◽  
Chie Miyazaki ◽  
Tsutomu Kajino ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Mesoporous Silica ◽  
Pore Size ◽  
Organic Solvents ◽  
Surface Characteristics ◽  
Immobilized Enzymes

scholarly journals Different methods and carriers for immobilization cellulase from Trichoderma viride and its remaining activity

2017 ◽  
Vol 4 (1) ◽  
pp. 9 ◽  
Author(s):  
Abdul Sattar Jabbar Taha
Keyword(s):  
Catalytic Activity ◽  
Cation Exchange ◽  
Anion Exchanger ◽  
Specific Activity ◽  
Trichoderma Viride ◽  
Immobilized Enzymes ◽  
Suitable Method ◽  
Native Enzyme

Objective: Many methods for enzymes immobilization and large number of carriers for immobilized enzymes, there are many benefits and diffeculties for immobilization, so the objective of this paper is to determine the suitable method and carrier for cellulase immobilization.Methods: Three methods used for immobilization which they adsorption, Glutaraldehyde and modified glutaraldehyde using two different carriers the first anion exchanger AM-21-A, and the second cation exchange fiber VION KN -1.Results: The result shows that the degree of saving catalytic activity for immobilized and free cellulase were 35, 55, and 75% for the three methods respectively and The result of degree maintain of specific activity for native enzyme were 57%, 42%, for the two carriers VION KN-1, AM-21-A respectively.Conclusions: It can be concluded that the modified glutaraldehyde is the best method for cellulase immobilization and VION KN-1 is better carrier than AM-21-A.

Electrochemical control of the catalytic activity of immobilized enzymes

2020 ◽  
Vol 56 (89) ◽  
pp. 13800-13803
Author(s):  
Vasantha Krishna Kadambar ◽  
Madhura Bellare ◽  
Paolo Bollella ◽  
Evgeny Katz ◽  
Artem Melman
Keyword(s):  
Catalytic Activity ◽  
Carbon Nanotube ◽  
Immobilized Enzymes ◽  
Electrochemical Reactions ◽  
Electrochemical Control ◽  
Activity Of Enzymes ◽  
Local Ph

Regulation of the catalytic activity of enzymes immobilized on carbon nanotube electrodes was achieved by changing their local pH environment using electrochemical reactions.

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