High Carbonyl Content Oxidized Starch Prepared by Hydrogen Peroxide and Its Thermoplastic Application

2009 ◽  
Vol 61 (11) ◽  
pp. 646-655 ◽  
Author(s):  
Shui-Dong Zhang ◽  
Yu-Rong Zhang ◽  
Xiu-Li Wang ◽  
Yu-Zhong Wang
Keyword(s):  
Hydrogen Peroxide ◽  
Carbonyl Content ◽  
Oxidized Starch

Effect of the carbonyl content on the properties of composite films based on oxidized starch and gelatin

2013 ◽  
Vol 130 (5) ◽  
pp. 3809-3815 ◽  
Author(s):  
Yajuan Wang ◽  
Lan Jiang ◽  
Jingkuan Duan ◽  
Shuangxi Shao
Keyword(s):  
Composite Films ◽  
Carbonyl Content ◽  
Oxidized Starch

Preparation of highly-oxidized starch using hydrogen peroxide and its application as a novel ligand for zirconium tanning of leather

2017 ◽  
Vol 174 ◽  
pp. 823-829 ◽  
Author(s):  
Yue Yu ◽  
Ya-nan Wang ◽  
Wei Ding ◽  
Jianfei Zhou ◽  
Bi Shi
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidized Starch

Effect of carbonyl content on the properties of thermoplastic oxidized starch

2009 ◽  
Vol 78 (1) ◽  
pp. 157-161 ◽  
Author(s):  
Yu-Rong Zhang ◽  
Shui-Dong Zhang ◽  
Xiu-Li Wang ◽  
Rong-Yi Chen ◽  
Yu-Zhong Wang
Keyword(s):  
Carbonyl Content ◽  
Oxidized Starch

scholarly journals Preparation and properties of hydrogen peroxide oxidized starch for industrial use

2020 ◽  
Vol 74 (1) ◽  
pp. 25-36
Author(s):  
Natasa Karic ◽  
Jelena Rusmirovic ◽  
Maja Djolic ◽  
Tihomir Kovacevic ◽  
Ljiljana Pecic ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Industrial Process ◽  
Optimization Procedure ◽  
Morphological Properties ◽  
Complex Catalyst ◽  
Oxidized Starch ◽  
Paper Manufacturing ◽  
Starch Oxidation ◽  
Sunflower Oils ◽  
Industrial Use

Oxidized starch, an additive used in paper manufacturing and products for construction industry, is usually produced using harmful oxidant, such as hypochlorites or periodates. In this study, a simple and efficient eco-friendly laboratory and industrial procedures for starch oxidation were developed. The procedure involves application of small amounts of more environmentally friendly oxidant, hydrogen peroxide, a novel special metal complex catalyst such as copper(II) citrate and copper(II) ricinoleate and biobased plasticizers. Optimization procedure, with respect to the quantity of hydrogen peroxide and temperature in the presence of iron(II) sulphate catalyst, was performed by using the response surface methodology. Compa-rative analysis of the use of the other catalysts that is copper(II) sulphate, copper(II) citrate and copper(II) ricinoleate, indicated copper(II) citrate as the catalyst of choice. Improvement of starch is achieved using three plasticizers: ricinoleic acid (RA), diisopropyl tartarate, as well as epoxidized soybean, linseed and sunflower oils. The effects of hydrogen peroxide and catalyst concentrations, as well as the reaction temperature in the presence of naturally based plasticizers on the physicochemical, thermal and morphological properties of oxidized starch are presented. According to the results obtained in initial experiments, the optimal industrial process is based on the use of copper(II) citrate (0.1 %) as a catalyst and RA (3 %) as a plasticizer.

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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