Yue Cui
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Yue Cui has a total of 2 co-authors. Here are the top co-authors by number of shared publications:
- John Patrick Barford
Department of Chemical and Biomolecular Engineering, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong
9 shared publications Reinhard Renneberg
Department of Department of Chemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China
9 shared publications
Latest Publications
- 15 November 2007
- Published by Elsevier in Sensors and Actuators B: Chemical
- Vol. 127 (2) , 358-361
Development of an l-glutamate biosensor using the coimmobilization of l-glutamate dehydrogenase and p-hydroxybenzoate hydroxylase on a Clark-type electrode
- 15 November 2007
- Published by Elsevier in Sensors and Actuators B: Chemical
- Vol. 127 (2) , 358-361
Development of an l-glutamate biosensor using the coimmobilization of l-glutamate dehydrogenase and p-hydroxybenzoate hydroxylase on a Clark-type electrode
- 29 October 2007
- Published by Taylor & Francis in Analytical Letters
- Vol. 40 (15) , 2915-2924
Gas Chromatographic Determination of Poly(3‐hydroxybutyrate) with Alkaline Hydrolysis and Acid Esterification
A new pretreatment method for the gas chromatographic determination of poly(3‐hydroxybutyrate) (PHB) was developed based on a combination of alkaline hydrolysis and acid esterification. The determination principle is as follows: PHB is hydrolyzed to its monomer 3‐hydroxybutyrate by alkaline solution, followed by the esterification with methanol to generate the methyl ester of 3‐hydroxybutyrate catalyzed by acid, which is detected by a gas chromatography. From the comparison of effects of alkali and acid on PHB hydrolysis and 3‐hydroxybutyrate esterification, alkali resulted in a better performance for the hydrolysis, while acid was better for the esterification. The pretreatment conditions for PHB were optimized and the determination performance was characterized.
- 29 October 2007
- Published by Taylor & Francis in Analytical Letters
- Vol. 40 (15) , 2915-2924
Gas Chromatographic Determination of Poly(3‐hydroxybutyrate) with Alkaline Hydrolysis and Acid Esterification
A new pretreatment method for the gas chromatographic determination of poly(3‐hydroxybutyrate) (PHB) was developed based on a combination of alkaline hydrolysis and acid esterification. The determination principle is as follows: PHB is hydrolyzed to its monomer 3‐hydroxybutyrate by alkaline solution, followed by the esterification with methanol to generate the methyl ester of 3‐hydroxybutyrate catalyzed by acid, which is detected by a gas chromatography. From the comparison of effects of alkali and acid on PHB hydrolysis and 3‐hydroxybutyrate esterification, alkali resulted in a better performance for the hydrolysis, while acid was better for the esterification. The pretreatment conditions for PHB were optimized and the determination performance was characterized.
- 21 May 2007
- Published by Elsevier in Sensors and Actuators B: Chemical
- Vol. 123 (2) , 696-700
Development of an interference-free biosensor for glucose-6-phosphate using a bienzyme-based Clark-type electrode
- 21 May 2007
- Published by Elsevier in Sensors and Actuators B: Chemical
- Vol. 123 (2) , 696-700
Development of an interference-free biosensor for glucose-6-phosphate using a bienzyme-based Clark-type electrode
- 1 May 2007
- Published by Elsevier in Biosensors and Bioelectronics
- Vol. 22 (11) , 2754-2758
Development of a glucose-6-phosphate biosensor based on coimmobilized p-hydroxybenzoate hydroxylase and glucose-6-phosphate dehydrogenase
- 1 May 2007
- Published by Elsevier in Biosensors and Bioelectronics
- Vol. 22 (11) , 2754-2758
Development of a glucose-6-phosphate biosensor based on coimmobilized p-hydroxybenzoate hydroxylase and glucose-6-phosphate dehydrogenase
- Open Access
- 2 October 2006
- Published by Springer Nature in Analytical Sciences
- Vol. 22 (10) , 1279-1281
A Disposable, Screen-Printed Electrode for the Amperometric Determination of Azide Based on the Immobilization with Catalase or Tyrosinase
A disposable, screen-printed electrode based on the immobilization of catalase or tyrosinase was developed to construct biosensors for the amperometric determination of azide. The determination principles for azide by these two methods are based on inhibiting the enzymatic consumption of an electrode-detectable substance (hydrogen peroxide or catechol) on an enzyme-immobilized electrode. Both of these methods show a sensitive detection range and a short measuring time.
- 2 October 2006
- Published by Springer Nature in Analytical Sciences
- Vol. 22 (10) , 1279-1281
Open AccessA Disposable, Screen-Printed Electrode for the Amperometric Determination of Azide Based on the Immobilization with Catalase or Tyrosinase
A disposable, screen-printed electrode based on the immobilization of catalase or tyrosinase was developed to construct biosensors for the amperometric determination of azide. The determination principles for azide by these two methods are based on inhibiting the enzymatic consumption of an electrode-detectable substance (hydrogen peroxide or catechol) on an enzyme-immobilized electrode. Both of these methods show a sensitive detection range and a short measuring time.
- Open Access
- 2 October 2006
- Published by Springer Nature in Analytical Sciences
- Vol. 22 (10) , 1323-1326
Determination of Poly(3-hydroxybutyrate) Using a Combination of Enzyme-based Biosensor and Alkaline Hydrolysis
The combination of an enzyme-based biosensor and alkaline hydrolysis was developed for the measurement of poly(3-hydroxybutyrate) (PHB). The principle of the determination is based on that the alkaline condition converts PHB to produce its monomer, 3-hydroxybutyrate (3-HB), which generates a detectable current signal by an amperometric biosensor through coupled two-enzyme reactions on an electrode. This method takes less than 40 min, and results in a linear detection range of 0.5 - 110 mg L-1 PHB with a detection limit of 0.3 mg L-1 by the saturated production of 3-HB; it can also take less than 15 min and result in a linear detection range of 1.0 - 160 mg L-1 PHB with a detection limit of 0.5 mg L-1 by a part production of 3-HB. The method also shows simple operation and high reproducibility.
- 2 October 2006
- Published by Springer Nature in Analytical Sciences
- Vol. 22 (10) , 1323-1326
Open AccessDetermination of Poly(3-hydroxybutyrate) Using a Combination of Enzyme-based Biosensor and Alkaline Hydrolysis
The combination of an enzyme-based biosensor and alkaline hydrolysis was developed for the measurement of poly(3-hydroxybutyrate) (PHB). The principle of the determination is based on that the alkaline condition converts PHB to produce its monomer, 3-hydroxybutyrate (3-HB), which generates a detectable current signal by an amperometric biosensor through coupled two-enzyme reactions on an electrode. This method takes less than 40 min, and results in a linear detection range of 0.5 - 110 mg L-1 PHB with a detection limit of 0.3 mg L-1 by the saturated production of 3-HB; it can also take less than 15 min and result in a linear detection range of 1.0 - 160 mg L-1 PHB with a detection limit of 0.5 mg L-1 by a part production of 3-HB. The method also shows simple operation and high reproducibility.
- 1 September 2006
- Published by Taylor & Francis in Analytical Letters
- Vol. 39 (12) , 2429-2439
Determination of Poly(3?Hydroxybutyrate) using a Combination of Enzymatic Spectrophotometry and Alkaline Hydrolysis
A combination of enzyme‐based spectrophotometric analysis and alkaline hydrolysis was developed for the measurement of poly(3‐hydroxybutyrate) (PHB). The principle of the determination is as follows: alkaline hydrolysis decomposes PHB into its monomer product 3‐hydroxybutyrate, which is followed with enzymatic reaction catalyzed by 3‐hydroxybutyrate dehydrogenase in the presence of nicotinamide adenosine dinucleotide (NAD). The product, nicotinamide adenosine dinucleotide with hydrogen (NADH) results in a spectrophotometric signal at 340 nm. This method shows high performance characteristics with simple operations.
- 1 September 2006
- Published by Taylor & Francis in Analytical Letters
- Vol. 39 (12) , 2429-2439
Determination of Poly(3?Hydroxybutyrate) using a Combination of Enzymatic Spectrophotometry and Alkaline Hydrolysis
A combination of enzyme‐based spectrophotometric analysis and alkaline hydrolysis was developed for the measurement of poly(3‐hydroxybutyrate) (PHB). The principle of the determination is as follows: alkaline hydrolysis decomposes PHB into its monomer product 3‐hydroxybutyrate, which is followed with enzymatic reaction catalyzed by 3‐hydroxybutyrate dehydrogenase in the presence of nicotinamide adenosine dinucleotide (NAD). The product, nicotinamide adenosine dinucleotide with hydrogen (NADH) results in a spectrophotometric signal at 340 nm. This method shows high performance characteristics with simple operations.
- 10 August 2006
- Published by Springer Nature in Analytical and Bioanalytical Chemistry
- Vol. 386 (5) , 1567-1570
Development of a bienzyme system for the electrochemical determination of nitrate in ambient air
This work reports the development of a bienzyme system consisting of salicylate hydroxylase (SHL) and nitrate reductase (NaR) for the electrochemical determination of nitrate. This method measures the concentration of nitrate directly under ambient air without suffering from oxygen interferences. The determination is based on the detection of NADH consumption, and the principle is as follows: NADH initiates the irreversible decarboxylation and hydroxylation of salicylate by SHL in the presence of oxygen to produce catechol, which results in a detectable signal due to its oxidation at the working electrode; the second enzyme, NaR, in the presence of nitrate, reduced the availability of NADH, and consequently, the current difference after the injection of nitrate is proportional to its concentration. This method shows high performance characteristics for nitrate determination with a broad detection range between 10 μM and 1,000 μM, a short measuring time of around 5 min, and a simple operation without sample pretreatment by inert gas purge or oxygen scavenger.
- 10 August 2006
- Published by Springer Nature in Analytical and Bioanalytical Chemistry
- Vol. 386 (5) , 1567-1570
Development of a bienzyme system for the electrochemical determination of nitrate in ambient air
This work reports the development of a bienzyme system consisting of salicylate hydroxylase (SHL) and nitrate reductase (NaR) for the electrochemical determination of nitrate. This method measures the concentration of nitrate directly under ambient air without suffering from oxygen interferences. The determination is based on the detection of NADH consumption, and the principle is as follows: NADH initiates the irreversible decarboxylation and hydroxylation of salicylate by SHL in the presence of oxygen to produce catechol, which results in a detectable signal due to its oxidation at the working electrode; the second enzyme, NaR, in the presence of nitrate, reduced the availability of NADH, and consequently, the current difference after the injection of nitrate is proportional to its concentration. This method shows high performance characteristics for nitrate determination with a broad detection range between 10 μM and 1,000 μM, a short measuring time of around 5 min, and a simple operation without sample pretreatment by inert gas purge or oxygen scavenger.
- 1 July 2006
- Published by Elsevier in Analytical Biochemistry
- Vol. 354 (1) , 162-164
Amperometric determination of phosphoglucomutase activity with a bienzyme screen-printed biosensor
- 1 July 2006
- Published by Elsevier in Analytical Biochemistry
- Vol. 354 (1) , 162-164
Amperometric determination of phosphoglucomutase activity with a bienzyme screen-printed biosensor