Amperometric determination of phosphate by use of a nucleoside phosphorylase-xanthine oxidase enzyme sensor based on a clark-type hydrogen peroxide or oxygen electrode

1990 ◽  
Vol 191 (1) ◽  
pp. 106-109 ◽  
Author(s):  
Stephan D. Haemmerli ◽  
Ahmad A. Suleiman ◽  
George G. Guilbault
Keyword(s):  
Hydrogen Peroxide ◽  
Xanthine Oxidase ◽  
Oxygen Electrode ◽  
Amperometric Determination ◽  
Nucleoside Phosphorylase ◽  
Enzyme Sensor ◽  
Oxidase Enzyme

Bilayer lipid membrane biosensor with enhanced stability for amperometric determination of hydrogen peroxide

Talanta ◽  
2011 ◽  
Vol 85 (1) ◽  
pp. 43-48 ◽  
Author(s):  
Longzhen Zheng ◽  
Leyan Xiong ◽  
Dan Zheng ◽  
Yindi Li ◽  
Qiang Liu ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Lipid Membrane ◽  
Bilayer Lipid Membrane ◽  
Amperometric Determination ◽  
Bilayer Lipid ◽  
Enhanced Stability

Fabrication of cuprous sulfide nanorods supported on copper foam for nonenzymatic amperometric determination of glucose and hydrogen peroxide

RSC Advances ◽  
2016 ◽  
Vol 6 (93) ◽  
pp. 90732-90738 ◽  
Author(s):  
Wangdong Lu ◽  
Yujing Sun ◽  
Haichao Dai ◽  
Pengjuan Ni ◽  
Shu Jiang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Amperometric Determination ◽  
Copper Foam ◽  
Cuprous Sulfide

Cuprous sulfide nanothorns were fabricated on copper foam for nonenzymatic amperometric determination of glucose and hydrogen peroxide.

scholarly journals Enzymic determination of inorganic phosphates, organic phosphates and phosphate-liberating enzymes by use of nucleoside phosphorylase-xanthine oxidase (dehydrogenase)-coupled reactions

1985 ◽  
Vol 230 (1) ◽  
pp. 255-260 ◽  
Author(s):  
H de Groot ◽  
H de Groot ◽  
T Noll
Keyword(s):  
Uric Acid ◽  
Xanthine Oxidase ◽  
High Sensitivity ◽  
Inorganic Pyrophosphatase ◽  
Enzyme Assays ◽  
Tetrazolium Salt ◽  
Nucleoside Phosphorylase ◽  
Organic Phosphates ◽  
Inorganic Phosphates

Coupled enzyme assays are described for measuring inorganic phosphates, organic phosphates and phosphate-liberating enzymes in biological material. The assays all determine Pi by its reaction with inosine, catalysed by nucleoside phosphorylase; this yields ribose 1-phosphate and hypoxanthine. The hypoxanthine is oxidized to uric acid by xanthine oxidase, and may be measured either by the absorbance of the uric acid, or by the formazan formed when a tetrazolium salt is used as the oxidant. The coupled enzyme assays are characterized by high sensitivity, quantitative utilization of phosphates and stoichiometric formation of the measurable products, measurement at pH 6.0-8.5, determination of phosphates within a single analytical step, and continuous measurement of phosphohydrolase activity in a corresponding rate assay. Examples include determinations of substrates such as Pi, PPi and AMP, and of enzymes such as 5′-nucleotidase, inorganic pyrophosphatase and glucose-6-phosphatase. Directions for further examples are given.

Determination of Aspartame in Beverages Using an Alcohol Oxidase Enzyme Electrode

1989 ◽  
Vol 72 (1) ◽  
pp. 30-33
Author(s):  
Vicki J Smith ◽  
Richard A Green ◽  
Thomas R Hopkins
Keyword(s):  
Liquid Chromatography ◽  
Standard Deviation ◽  
Methyl Ester ◽  
Alcohol Oxidase ◽  
Ester Group ◽  
Oxygen Electrode ◽  
Artificial Sweetener ◽  
Relative Standard ◽  
Oxidase Enzyme

Abstract A new method for the determination of the artificial sweetener aspartame is described. α-Chymotrypsin is used to cleave the methyl ester group of aspartame, producing methanol hydrolytically. The methanol is detected using an electrode which is constructed by physically trapping yeast alcohol oxidase enzyme at the tip of a dissolved oxygen electrode. The decrease in oxygen concentration, which occurs as methanol is enzymatically oxidized to formaldehyde, is measured amperometrically. Aspartame levels in diet soft drinks as determined by the proposed method and by liquid chromatography are in excellent agreement. The relative standard deviation of the measurements is 0.83%. The methanol present in diet cola as a result of aspartame degradation can also be measured by using the electrode without α-chymotrypsin.

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