scholarly journals Mineralization of Hydrochlorothiazide using Hydrogen Peroxide in Subcritical Water

Author(s):  
Erdal Yabalak ◽  
Özkan Görmez ◽  
Yahya Nural
Desalination ◽  
2011 ◽  
Vol 274 (1-3) ◽  
pp. 200-205 ◽  
Author(s):  
Vasileia M. Daskalaki ◽  
Eleni S. Timotheatou ◽  
Alexandros Katsaounis ◽  
Dimitrios Kalderis

2015 ◽  
Vol 54 (35) ◽  
pp. 8650-8658 ◽  
Author(s):  
Hisao Hori ◽  
Hirotaka Tanaka ◽  
Kengo Watanabe ◽  
Takahiro Tsuge ◽  
Takehiko Sakamoto ◽  
...  

Author(s):  
Zeynep Bilici ◽  
Mohammed Saleh ◽  
Erdal Yabalak ◽  
Alireza Khataee ◽  
Nadir Dizge

Abstract Wastewater from the textile industry containing a high concentration of organic and inorganic chemicals have strong color and residual chemical oxygen demand (COD). Therefore, advanced oxidation processes (AOPs) are very good candidates to treat textile industry wastewater. In this study, we investigated the effect of different types of AOPs supported with hydrogen peroxide (H2O2) on the treatment of viscose fibers dyeing wastewater. Fenton, photo-Fenton, and Fenton supported subcritical water oxidation (FSWO) processes were chosen as AOPs to compare the treatment efficiency of viscose fibers dyeing wastewater. The effects of solution pH, Fe2+ concentration, and H2O2 concentration on the treatment of viscose fibers dyeing wastewater were tested. The maximum color and COD removal efficiency was obtained corresponding to pH 2.5 for all oxidation methods when MB dye solution was used. However, the maximum efficiencies were obtained at pH 3.0 for real textile wastewater decolorization. The MB dye removal efficiency was increased to 97.22, 100, and 100% for Fenton, photo-Fenton, and FSWO processes, respectively, when the addition of H2O2 concentration was adjusted to 125 mg/L. However, the maximum color removal efficiencies of viscose fibers dyeing wastewater were obtained 56.94, 61.26, 64.11% for Fenton, photo-Fenton, FSWO processes, respectively. As a result, the FSWO showed maximum color removal efficiencies.


2013 ◽  
Vol 92 (4) ◽  
pp. 615-622 ◽  
Author(s):  
Somayeh Daneshvar ◽  
Nakamura Hidemi ◽  
Feridoun Salak ◽  
Nader Mahinpey

2019 ◽  
Vol 84 (7) ◽  
pp. 757-767 ◽  
Author(s):  
Erdal Yabalak ◽  
İpek Topaloğlu ◽  
Ahmet Gizir

Degradation of epichlorohydrin was investigated using subcritical water oxidation method in the presence of hydrogen peroxide. Degradation rate was monitored by means of total organic carbon (TOC) analysis. The central composite design was used to determine optimal TOC removal conditions and modelling experimental process. The effects of all experimental variables (temperature, oxidant concentration of hydrogen peroxide and treatment time) on the TOC removal rates were evaluated and the theoretical prediction model was proposed. Reliability of the employed model was evaluated using ANOVA. F value and the p-value of the model were found to be 84.60 and <0.0001, respectively. 93.78 % of TOC removal was achieved in the degradation of epichlorohydrin at 373 K of temperature and 75 min of treatment time using 90 mM of H2O2.


Author(s):  
George E. Childs ◽  
Joseph H. Miller

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.


2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

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 &gt;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.


2010 ◽  
Vol 34 (8) ◽  
pp. S27-S27
Author(s):  
Xueling Dai ◽  
Ping Chang ◽  
Ke Xu ◽  
Changjun Lin ◽  
Hanchang Huang ◽  
...  

2020 ◽  
Vol 48 (2) ◽  
pp. 613-620
Author(s):  
Clara Ortegón Salas ◽  
Katharina Schneider ◽  
Christopher Horst Lillig ◽  
Manuela Gellert

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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