Chemicals used for treatment of water intended for human consumption. Hydrogen peroxide

2009 ◽  
Keyword(s):  
Hydrogen Peroxide ◽  
Human Consumption

scholarly journals Studies on the Preservation of Raw Cow’s Milk by Chemical Method

1970 ◽  
Vol 42 (3) ◽  
pp. 317-326 ◽  
Author(s):  
F Rokhsana ◽  
UK Das ◽  
R Yeasmin ◽  
A Nahar ◽  
S Parveen
Keyword(s):  
Hydrogen Peroxide ◽  
Chemical Method ◽  
Room Temperature ◽  
Storage Period ◽  
Total Coliform ◽  
Human Consumption ◽  
Milk Products ◽  
E Coli ◽  
Keeping Quality ◽  
Control Milk

Studies carried out to develop a technique for the preservation of cow's milk in raw condition using hydrogen peroxide (H2O2) as a preservative. Fresh cow’s milk was collected and experiments were conducted by four treatments in order to achieve the optimum condition of storage. The treatments were with various concentration of H2O2 starting from 0.05 %, 0.1 %, 0.2 %, 0.3 %, 0.4 %, & 0.5 %. Treated milk with 0.05 % concentration of H2O2 had storage period of 20 days compared to that of the control one (5 days only) in refrigerated temperature (±8°C). On the other hand hydrogen peroxide treated milk (0.05 %) had a storage period of 8 hours at room temperature (±28°C). Results also showed that the higher concentration of H2O2 had no effect on storage period than that of control. Milk products like kheer and halawa prepared by treated milk and stored for 20 days showed almost nil growth of total coliform and E. coli which means that food products prepared from hydrogen peroxide treated milk is safe for human consumption. Key words: Raw, Storage, Hydrogen peroxide, Preservative, keeping quality, Pasteurization, deteriorated, MPN. Bangladesh J. Sci. Ind. Res. 42(3), 317-326, 2007

scholarly journals DEGRADATION OF THE ANTIBIOTIC METRONIDAZOLE BY ADVANCED OXIDATIVE PROCESSES

2017 ◽  
Vol 14 (28) ◽  
pp. 72-86
Author(s):  
Schirlei Diana Kleinubing SILVA ◽  
Salah Din Mahmud HASAN ◽  
Maurício Ferreira ROSA
Keyword(s):  
Hydrogen Peroxide ◽  
Sewage Treatment ◽  
Artemia Salina ◽  
Heterogeneous Photocatalysis ◽  
The Body ◽  
Human Consumption ◽  
Original Form ◽  
Biological Degradation ◽  
Economic Sectors ◽  
Oxidative Processes

The pharmaceutical industry is one of the fastest growing economic sectors in the world. The existence of medicines for the most different diseases has made the use of these products grow vertiginously in recent years. When ingested these compounds are partially absorbed by the body, and part excreted in its original form. Sewage treatment plants (ETS), with processes based on biological degradation, can not remove these drugs from water. When it is returned to the environment, or intended for human consumption, this water contains small amounts of these compounds, which can cause deleterious effects to both humans and the environment. In this situation the use of photocatalytic methods can be an important alternative in the removal of these contaminants from the aquatic environment. This work studied the photodegradation of the antibiotic metronidazole (MNZ) in aqueous solution by photolytic and photocatalytic methods (POA) using ultraviolet light, hydrogen peroxide (H2O2) and titanium dioxide (TiO2). To investigate the photocatalytical process, an experimental design 23 was performed to evaluate the influence of the variables pH, hydrogen peroxide concentration and TiO2 concentration over the photodegradation of drug, which was spectrophotometrycally monitored in the UV-VIS region. The kinetic model of pseudofirst order described quite well the degradation behavior of the drug. The photocatalytical process only in presence of H2O2, the highest rate of degradation obtained was 8.66% at pH 4. In the heterogeneous photocatalysis experiments the highest degradation rate of the MNZ was 72.1% when TiO2 was used in concentration of 100 mg∙L-1, H2O2 at the concentration of 1000 mg∙L-1 at pH 10. The statistical analysis of the results showed that in the heterogeneous photocatalysis experiments with TiO2 only the pH/H2O2 interaction had no significant effect. Cytotoxicity assays employing Artemia salina as bioindicator showed a 90% reduction in sample toxicity after the photocatalytical treatment.

scholarly journals Deteksi Kandungan Nitrit dan Hidrogen Peroksida dalam Produk Sarang Burung Walet Bersih Asal Indonesia

2021 ◽  
Vol 10 (1) ◽  
pp. 20
Author(s):  
Siti Gusti Ningrum
Keyword(s):  
Public Health ◽  
Hydrogen Peroxide ◽  
Rapid Test ◽  
Human Consumption ◽  
Health Consequences ◽  
Low Concentration ◽  
New Information ◽  
Edible Bird’S Nest ◽  
Potential Public Health

The objective was to investigate nitrite contents of edible bird’s nest product for human consumption. The investigated edible bird’s nest included 19 samples from multiple lots of commercially local products. Nitrite concentrations were determined by spectrophotometry. Nitrite was detected in low concentration (10.752±1.515 ppm). Detection of adulteration which is residue of hydrogen peroxide was conducted in the present study. Hydrogen peroxide was detected by rapid test which specific for hydrogen peroxide. From 19 sample tested, there was no residue of hydrogen peroxide contained in the products. These results provide new information for evaluating nitrite and hydrogen peroxide in local edible bird’s nest products regarding potential public health consequences.

Peroxidase Localization in Hartmanella Trophozoites

1971 ◽  
Vol 29 ◽  
pp. 346-347 ◽  
Author(s):  
George E. Childs ◽  
Joseph H. Miller
Keyword(s):  
Hydrogen Peroxide ◽  
Ultrastructural Localization ◽  
Pathogenic Strain ◽  
Oxidative Enzymes ◽  
Differential Centrifugation ◽  
Electron Microscopic ◽  
Microscopic Studies ◽  
The Subject ◽  
Axenic Cultures

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

Protective effect of chitooligosaccharides on hydrogen peroxide-induced PC-12 cells death by inhibition of oxidative damage

2010 ◽  
Vol 34 (8) ◽  
pp. S27-S27
Author(s):  
Xueling Dai ◽  
Ping Chang ◽  
Ke Xu ◽  
Changjun Lin ◽  
Hanchang Huang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidative Damage ◽  
Protective Effect ◽  
Pc 12 Cells ◽  
Cells Death

Signal-regulated oxidation of proteins via MICAL

2020 ◽  
Vol 48 (2) ◽  
pp. 613-620
Author(s):  
Clara Ortegón Salas ◽  
Katharina Schneider ◽  
Christopher Horst Lillig ◽  
Manuela Gellert
Keyword(s):  
Signal Transduction ◽  
Hydrogen Peroxide ◽  
Cell Death ◽  
Redox Regulation ◽  
Signal Transduction Pathways ◽  
Cellular Functions ◽  
Intracellular Signals ◽  
Amino Acid Side Chains ◽  
Specific Receptors ◽  
Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

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