Chloride-accelerated Cu-Fenton chemistry for biofilm removal

2017 ◽  
Vol 53 (43) ◽  
pp. 5862-5865 ◽  
Author(s):  
Li Wang ◽  
Yanni Miao ◽  
Mingsheng Lu ◽  
Zhi Shan ◽  
Shan Lu ◽  
...  

Chloride ions dramatically enhance the antibacterial and anti-biofilm capability of Cu-based Fenton reagents.

2021 ◽  
Author(s):  
Li Wang ◽  
Rui Peng ◽  
Xue Liu ◽  
Chendi Heng ◽  
Yanni Miao ◽  
...  

Unwanted biofilms present challenges for many industries. Herein an innovative biofilm removal technology was developed based on nitrite-accelerated Fenton chemistry, where both dissolved Cu ions and nano-CuO surfaces efficiently generate...


2019 ◽  
Author(s):  
Andrew Carrier ◽  
Saher Hamid ◽  
David Oakley ◽  
Ken Oakes ◽  
Xu Zhang

<div><div><div><p>The Fenton reaction, the Fe-catalyzed conversion of hydrogen peroxide to reactive oxygen species (ROS) was discovered more than a century ago. It occurs widely in nature because of the ubiquity of Fenton reagents, i.e., Fe and H2O2, and ROS in environmental and biological systems; however, its mechanisms and the identity of the ROS generated under varying conditions have remained controversial. The widely accepted mechanism is that of successive oxidation and reduction of Fe2+ and Fe3+ by hydrogen peroxide to form ·OH and O2-·, respectively, where ·OH is implicated as the primary oxidant. However, the formation of high-valent Fe4+=O species has also been implicated. Herein, by systematically dissecting the contributions of various ROS species generated in the classical Fenton reaction by using specific ROS traps and scavengers, we identified that singlet oxygen (1O2) is the main ROS from pH 4–7. In contrast, although ·OH is produced in measurable quantities, it was not a major contributor to the oxidation of organic molecules.</p></div></div></div>


2019 ◽  
Author(s):  
Andrew Carrier ◽  
Saher Hamid ◽  
David Oakley ◽  
Ken Oakes ◽  
Xu Zhang

<div><div><div><p>The Fenton reaction, the Fe-catalyzed conversion of hydrogen peroxide to reactive oxygen species (ROS) was discovered more than a century ago. It occurs widely in nature because of the ubiquity of Fenton reagents, i.e., Fe and H2O2, and ROS in environmental and biological systems; however, its mechanisms and the identity of the ROS generated under varying conditions have remained controversial. The widely accepted mechanism is that of successive oxidation and reduction of Fe2+ and Fe3+ by hydrogen peroxide to form ·OH and O2-·, respectively, where ·OH is implicated as the primary oxidant. However, the formation of high-valent Fe4+=O species has also been implicated. Herein, by systematically dissecting the contributions of various ROS species generated in the classical Fenton reaction by using specific ROS traps and scavengers, we identified that singlet oxygen (1O2) is the main ROS from pH 4–7. In contrast, although ·OH is produced in measurable quantities, it was not a major contributor to the oxidation of organic molecules.</p></div></div></div>


Author(s):  
Al W. Stinson

The stratified squamous epithelium which lines the ruminal compartment of the bovine stomach performs at least three important functions. (1) The upper keratinized layer forms a protective shield against the rough, fibrous, constantly moving ingesta. (2) It is an organ of absorption since a number of substances are absorbed directly through the epithelium. These include short chain fatty acids, potassium, sodium and chloride ions, water, and many others. (3) The cells of the deeper layers metabolize butyric acid and to a lesser extent propionic and acetic acids which are the fermentation products of rumen digestion. Because of the functional characteristics, this epithelium is important in the digestive process of ruminant species which convert large quantities of rough, fibrous feed into energy.Tissue used in this study was obtained by biopsy through a rumen fistula from clinically healthy, yearling holstein steers. The animals had been fed a typical diet of hay and grain and the ruminal papillae were fully developed. The tissue was immediately immersed in 1% osmium tetroxide buffered to a pH of 7.4 and fixed for 2 hrs. The tissue blocks were embedded in Vestapol-W, sectioned with a Porter-Blum microtome with glass knives and stained with lead hydroxide. The sections were studied with an RCA EMU 3F electron microscope.


Biofouling ◽  
2003 ◽  
Vol 19 (3) ◽  
pp. 159-168 ◽  
Author(s):  
Nadia Oulahal- Lagsir ◽  
Adele Martial- Gros ◽  
Marc Bonneauc ◽  
Loic Bluma

Biofouling ◽  
2003 ◽  
Vol 19 (3) ◽  
pp. 159-168 ◽  
Author(s):  
NADIA OULAHAL-LAGSIR ◽  
ADELE MARTIAL-GROS ◽  
MARC BONNEAU ◽  
LOIC BLUM

1984 ◽  
Vol 52 (03) ◽  
pp. 347-349 ◽  
Author(s):  
Daan W Traas ◽  
Bep Hoegee-de Nobel ◽  
Willem Nieuwenhuizen

SummaryNative human plasminogen, the proenzyme of plasmin (E. C. 3.4.21.7) occurs in blood in two well defined forms, affinity forms I and II. In this paper, the feasibility of separating these forms of human native plasminogen by affinity chromatography, is shown to be dependent on two factors: 1) the ionic composition of the buffer containing the displacing agent: buffers of varying contents of sodium, Tris, phosphate and chloride ions were compared, and 2) the type of adsorbent. Two adsorbents were compared: Sepharose-lysine and Sepharose-bisoxirane-lysine. Only in the phosphate containing buffers, irrespective of the type of adsorbent, the affinity forms can be separated. The influence of the adsorbent can be accounted for by a large difference in dissociation constants of the complex between plasminogen and the immobilized lysine.


2020 ◽  
Vol 61 (9) ◽  
pp. 1775-1781
Author(s):  
Li-Bin Niu ◽  
Shoichi Kosaka ◽  
Masaki Yoshida ◽  
Yusuke Suetake ◽  
Kazuo Marugame

Sign in / Sign up

Export Citation Format

Share Document