Methylene Blue-Induced Stabilization Effect of Adsorbed Glucose Oxidase on a Carbon-Felt Surface for Bioelectrocatalytic Activity

2012 ◽  
Vol 159 (5) ◽  
pp. F110-F118 ◽  
Author(s):  
Yue Wang ◽  
Yasushi Hasebe
Keyword(s):  
Methylene Blue ◽  
Glucose Oxidase ◽  
Carbon Felt ◽  
Stabilization Effect

scholarly journals Reduced graphene oxide-supported methylene blue nanocomposite as a glucose oxidase-mimetic for electrochemical glucose sensing

RSC Advances ◽  
2018 ◽  
Vol 8 (57) ◽  
pp. 32565-32573 ◽  
Author(s):  
Shaojun Yang ◽  
Daliang Liu ◽  
Qing Bo Meng ◽  
Shuyao Wu ◽  
Xi-Ming Song
Keyword(s):  
Methylene Blue ◽  
Graphene Oxide ◽  
Glucose Oxidase ◽  
Reduced Graphene Oxide ◽  
Electrocatalytic Activity ◽  
Glucose Sensor ◽  
Glucose Sensing ◽  
Reduced Graphene

A novel electrochemical glucose sensor based on methylene blue-reduced graphene oxide nanocomposite was constructed, and the sensor exhibited good glucose oxidase-mimetic electrocatalytic activity towards glucose and practical applicability.

METABOLISM OF MAMMALIAN ERYTHROCYTES: V. ROLE OF CATALASE IN THE OXIDATION OF RIBOSE-5-PHOSPHATE BY THE ERYTHROCYTE

1954 ◽  
Vol 32 (6) ◽  
pp. 644-654 ◽  
Author(s):  
Marc Francoeur ◽  
Orville F. Denstedt
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Glucose Oxidase ◽  
Anaerobic Conditions ◽  
Beef Liver ◽  
Aerobic Conditions

Ribose-5-phosphate has been found to be rapidly oxidized by the stroma-free hemolyzate of human, rat, and rabbit erythrocytes in the presence of ferricyanide under anaerobic conditions, or in the presence of methylene blue under aerobic conditions. Compounds resembling R-5-P, such as ribose, arabinose, xylose, glucose, glucose-6-phosphate, fructose-6-phosphate, and hexose diphosphate are not oxidized under these conditions. The oxidation does not involve DPN or TPN and it is completely inhibited by cyanide. The Ks is about 2 × 10−2 M. Under anaerobic conditions, in the presence of ferricyanide, the enzyme responsible for the oxidation is catalase. Purified catalase from beef liver or from rabbit erythrocytes yields the same results as the SFH from human, rat, or rabbit erythrocytes with respect to specificity, cyanide sensitivity, and the Ks value. Under aerobic conditions, catalase is responsible also for the oxidation of R-5-P, but the mechanism involves the peroxidase action of catalase. Catalase catalyzes the oxidation of R-5-P by hydrogen peroxide in the presence of a system which slowly generates hydrogen peroxide, such as the glucose–glucose oxidase or the hemoglobin – methylene blue systems.

Influence of remote plasma on PEDOT:PSS‐coated carbon felt for improved activity of glucose oxidase

2019 ◽  
Vol 137 (14) ◽  
pp. 48521 ◽  
Author(s):  
May Kahoush ◽  
Nemeshwaree Behary ◽  
Aurélie Cayla ◽  
Brigitte Mutel ◽  
Jinping Guan ◽  
...  
Keyword(s):  
Glucose Oxidase ◽  
Carbon Felt ◽  
Remote Plasma ◽  
Coated Carbon

scholarly journals Surface modification of carbon felt by cold remote plasma for glucose oxidase enzyme immobilization

2019 ◽  
Vol 476 ◽  
pp. 1016-1024 ◽  
Author(s):  
May Kahoush ◽  
Nemeshwaree Behary ◽  
Aurélie Cayla ◽  
Brigitte Mutel ◽  
Jinping Guan ◽  
...  
Keyword(s):  
Surface Modification ◽  
Glucose Oxidase ◽  
Enzyme Immobilization ◽  
Carbon Felt ◽  
Remote Plasma ◽  
Oxidase Enzyme

scholarly journals Understanding the role of glucose oxidase on carbon felt as electrodes in biocapacitor studies

2019 ◽  
Vol 42 (3) ◽  
Author(s):  
Rajendran Rajaram ◽  
Dharmaraj Karuppasamy ◽  
P Ragupathy ◽  
Jayaraman Mathiyarasu
Keyword(s):  
Glucose Oxidase ◽  
Carbon Felt

METABOLISM OF MAMMALIAN ERYTHROCYTES: V. ROLE OF CATALASE IN THE OXIDATION OF RIBOSE-5-PHOSPHATE BY THE ERYTHROCYTE

1954 ◽  
Vol 32 (1) ◽  
pp. 644-654 ◽  
Author(s):  
Marc Francoeur ◽  
Orville F. Denstedt
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Glucose Oxidase ◽  
Anaerobic Conditions ◽  
Beef Liver ◽  
Aerobic Conditions

Ribose-5-phosphate has been found to be rapidly oxidized by the stroma-free hemolyzate of human, rat, and rabbit erythrocytes in the presence of ferricyanide under anaerobic conditions, or in the presence of methylene blue under aerobic conditions. Compounds resembling R-5-P, such as ribose, arabinose, xylose, glucose, glucose-6-phosphate, fructose-6-phosphate, and hexose diphosphate are not oxidized under these conditions. The oxidation does not involve DPN or TPN and it is completely inhibited by cyanide. The Ks is about 2 × 10−2 M. Under anaerobic conditions, in the presence of ferricyanide, the enzyme responsible for the oxidation is catalase. Purified catalase from beef liver or from rabbit erythrocytes yields the same results as the SFH from human, rat, or rabbit erythrocytes with respect to specificity, cyanide sensitivity, and the Ks value. Under aerobic conditions, catalase is responsible also for the oxidation of R-5-P, but the mechanism involves the peroxidase action of catalase. Catalase catalyzes the oxidation of R-5-P by hydrogen peroxide in the presence of a system which slowly generates hydrogen peroxide, such as the glucose–glucose oxidase or the hemoglobin – methylene blue systems.

A novel glucose biosensor constructed by glucose oxidase immobilized with methylene blue intercalated layered lanthanum niobic acid nanocomposite

2014 ◽  
Vol 135 ◽  
pp. 39-42 ◽  
Author(s):  
Xiaobo Zhang ◽  
Liqun Shen ◽  
Mingyan Wang ◽  
Gaowa Siqin ◽  
Zhiwei Tong ◽  
...  
Keyword(s):  
Methylene Blue ◽  
Glucose Oxidase ◽  
Glucose Biosensor ◽  
Niobic Acid

Effects of methylene blue and methyl red mediators on performance of yeast based microbial fuel cells adopting polyethylenimine coated carbon felt as anode

2018 ◽  
Vol 396 ◽  
pp. 1-11 ◽  
Author(s):  
Marcelinus Christwardana ◽  
Domenico Frattini ◽  
Grazia Accardo ◽  
Sung Pil Yoon ◽  
Yongchai Kwon
Keyword(s):  
Methylene Blue ◽  
Fuel Cells ◽  
Microbial Fuel Cells ◽  
Methyl Red ◽  
Carbon Felt ◽  
Coated Carbon
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