scholarly journals Electrogeneration of hydrogen peroxide applied to the peroxide-mediated oxidation of (R)-limonene in organic media

2007 ◽  
Vol 10 (4) ◽  
pp. 0-0 ◽  
Author(s):  
Camilo Enrique La Rotta Hernandez ◽  
Diogo Simon Werberich ◽  
Marcio Contrucci Saraiva de Mattos ◽  
Eliane D Elia
Keyword(s):  
Hydrogen Peroxide ◽  
Organic Media ◽  
Mediated Oxidation

scholarly journals RuIII(edta) mediated oxidation of azide in the presence of hydrogen peroxide. Azide versus peroxide activation

2014 ◽  
Vol 43 (8) ◽  
pp. 3087-3094 ◽  
Author(s):  
Debabrata Chatterjee ◽  
Alicja Franke ◽  
Maria Oszajca ◽  
Rudi van Eldik
Keyword(s):  
Hydrogen Peroxide ◽  
Peroxide Activation ◽  
Mediated Oxidation

Controlled RAFT polymerization facilitated by a nanostructured enzyme mimic

2018 ◽  
Vol 9 (35) ◽  
pp. 4448-4454 ◽  
Author(s):  
Qiang Fu ◽  
Hadi Ranji-Burachaloo ◽  
Min Liu ◽  
Thomas G. McKenzie ◽  
Shereen Tan ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Hydroxyl Radicals ◽  
Raft Polymerization ◽  
Enzyme Mimic ◽  
Organic Media

A nanostructured MOF composite was utilized as an enzyme mimic for the generation of hydroxyl radicals from hydrogen peroxide, which can subsequently initiate RAFT polymerizations in aqueous or organic media.

scholarly journals Auto-Cross-Linking Hydrogels of Hydrogen Peroxide-Oxidized Pectin and Gelatin for Applications in Controlled Drug Delivery

2019 ◽  
Vol 2019 ◽  
pp. 1-11 ◽  
Author(s):  
Claudia A. Garrido ◽  
Michel Vargas ◽  
Jose F. Alvarez-Barreto
Keyword(s):  
Drug Delivery ◽  
Hydrogen Peroxide ◽  
Low Cost ◽  
Controlled Drug Delivery ◽  
Wound Dressings ◽  
Attractive Alternative ◽  
Swelling Properties ◽  
Degree Of Oxidation ◽  
Mediated Oxidation ◽  
Recent Attention

Pectin-based hydrogels for biomedical applications have attracted recent attention due to their low cost, large availability of the materials, and high levels of biocompatibility. Specifically, periodate-oxidized pectin has been combined with chitosan and gelatin to form different structures. However, hydrogen peroxide-mediated oxidation of pectin has not been studied for this application; furthermore, there is little information on the effect of the degree of oxidation on hydrogel characteristics nor has the feasibility of these systems as controlled drug delivery matrices been explored. Thus, the present work proposes to study the properties of gelatin-peroxide-oxidized pectin hydrogels as drug delivery systems in wound dressing applications. Combinations of pectin at different degrees of oxidation (high, low, and native pectin) and gelatin were analyzed and tested by swelling properties, reswelling from xerogel and aerogel forms, SEM, FTIR, and drug release. It was determined that hydrogels that contained oxidized pectin had improved swelling ratios and stability, at 32°C, compared to those with native pectin and only gelatin. The porosity of the oxidized pectin hydrogels allowed to have sustained and high release rates, which would make them an attractive alternative for wound dressings.

Haematoporphyrin enhances the peroxidase activity of haemoglobin

2000 ◽  
Vol 04 (02) ◽  
pp. 168-174 ◽  
Author(s):  
SUSMITA SIL ◽  
MANOJ KAR ◽  
ABHAY SANKAR CHAKRABORTI
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Conformational Change ◽  
Anticancer Drugs ◽  
Peroxidase Activity ◽  
Superoxide Anion ◽  
Spectrophotometric Study ◽  
Stoichiometric Ratio ◽  
Mediated Oxidation

The effect of haematoporphyrin, a component of some of the widely used anticancer drugs, on the peroxidase activity of haemoglobin has been studied. Haematoporphyrin increases the haemoglobin-catalysed hydrogen peroxide-mediated oxidation of o-dianisidine or NADH. Spectrophotometric study reveals that an interaction occurs between haemoglobin and haematoporphyrin which leads to a conformational change of the protein. The extent of enhanced peroxidase activity as well as conformational change of the protein vary in a positive manner with the stoichiometric ratio of haematoporphyrin/haemoglobin. An increase in the peroxidase activity of haemoglobin was also observed in the presence of superoxide dismutase, which catalysed the removal of superoxide anion generated during autoxidation of haemoglobin. Possible mechanisms underlying the relation between the conformational change of haemoglobin due to its interaction with haematoporphyrin and the enhanced peroxidase activity are discussed.

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