Preparation of Immobilized Cholinesterase for Use in Analytical Chemistry.

Bauman, Elven K.; Goodson, Louis H.; Guilbault, George G.; Kramer, David N.

doi:10.1021/ac60230a023

Cited by 87 publications

(9 citation statements)

References 18 publications

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“…A method for the immobilisation of cholinesterase comprising capture of an enzyme into a starch gel followed by impregnation of the gel into the PUF matrix has been proposed. 253 An analytical system in which an enzymic minireactor is combined with an electrochemical sensor within one unit has been developed 254 to determine toxic substances of the anticholinesterase action (for example, insecticides) in air and in liquid media. As the air or solution sample under analysis is pumped through the minireactor, the inhibitor is collected on the immobilised enzyme and inhibits it.…”

Section: Enzymic Methodsmentioning

confidence: 99%

Polyurethane foams in chemical analysis: sorption of various substances and its analytical applications

Дмитриенко¹,

Zolotov²

2002

Russ. Chem. Rev.

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Section: Enzymic Methodsmentioning

confidence: 99%

Polyurethane foams in chemical analysis: sorption of various substances and its analytical applications

Дмитриенко¹,

Zolotov²

2002

Russ. Chem. Rev.

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“…For this reason, the incubation interval of 5 min was chosen for further experiments, it was the maximum signal for the 300 times diluted tracer. From Figure 4 it follows that longer incubation intervals resulted in decreased signals, the accumulated thiocholine was consumed in the concurrent oxidation reaction with oxygen [30]. The other parameters affecting the immunoreaction (buffer type and pH, amount of immobilized MAb) were optimized.…”

Section: Optimization Of the Sensing System And Assay Conditionsmentioning

confidence: 99%

“…On the other hand, the neutral phosphate buffer could minimize the spontaneous hydrolysis of acetylthiocholine [30].…”

Section: Optimization Of the Sensing System And Assay Conditionsmentioning

confidence: 99%

Disposable multichannel immunosensors for 2,4‐dichlorophenoxyacetic acid using acetylcholinesterase as an enzyme label

Kaláb

Skládal

1997

Electroanalysis

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An improved version of the disposable multichannel immunochemical biosensor for the herbicide 2,4-dichlorophenoxyacetic acid (2,4-D) based on a screen-printed amperometric transducer and monoclonal antibodies (MAb) against 2,4-D is reported. Entrapment within a thin Nafion film was used for the direct immobilization of MAb at the electrode surface. The amount of the tracer (2,4-D conjugated to acetylcholinesterase) bound in a competitive immunochemical reaction was determined amperometrically using acetylthiocholine iodide as substrate. The measuring procedure (times of incubation with tracer and substrate, pH, tracer concentration) was optimized. The sensor was able to detect less than 0.01 pgL of free 2,4-D in water. One analysis (8 samples) was completed in 30 min (20min for immunochemical reaction, 5 min incubation with substrate, 5 min measurement). The performance of the immunosensor (two configurations) was evaluated on real samples (tap water) with added 2,4-D. The determined amounts (mean values 0.097 to 0.105 and 0.89 to 1.13) corresponded well with the added contents of 2,4-D (0.100 and 1.00 pgL, respectively).

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“…The functions of squeezing in the batch squeezer is similar to that of flowing of solution in the circulated flow reactor: (1) to bring fresh solution to contact with the enzyme film supported on the exterior and interior surfaces of PU foam; and (2) to reduce the aqueous film resistance on the enzyme film. Therefore, the same kinetic model could be used in both batch squeezer and circulated flow reactor.…”

Section: Theoretical Considerationsmentioning

confidence: 99%

Kinetic studies on urea hydrolysis by immobilized urease in a batch squeezer and flow reactor

Huang

Chen

1992

Biotech & Bioengineering

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The immobilization of urease on the reticulated polyurethane foam, and the kinetic phenomenon of urea hydrolysis by the resulting immobilized urease in both batch squeezer and circulated flow reactors were studied. Urease was immobilized with bovine serum albumin and glutaraldehyde on polyurethane foam support of 7 to 15 mum thickness. The residual apparent activity of urease after immobilization was about 50%. The good hydrodynamic property and flexibility of polyurethane foam were retained in solution after immobilization. A modified biofilm reactor model was used to describe the kinetic phenomenon of urea hydrolysis in both batch squeezer and circulated flow reactors. The characteristic parameters of the reactor model for both bioreactors were obtained by combining the Rosenbrock optimization method, the Rungs-Kutta method, and the Newton-Raphson method. The best-fit results were in good agreement with the experimental data. This study suggests another application of polyurethane foam in enzyme immobilization and immobilized enzyme reactors, which offers potential for practical applications in various bioreactors.

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Preparation of Immobilized Cholinesterase for Use in Analytical Chemistry.

Cited by 87 publications

References 18 publications

Polyurethane foams in chemical analysis: sorption of various substances and its analytical applications

Polyurethane foams in chemical analysis: sorption of various substances and its analytical applications

Disposable multichannel immunosensors for 2,4‐dichlorophenoxyacetic acid using acetylcholinesterase as an enzyme label

Kinetic studies on urea hydrolysis by immobilized urease in a batch squeezer and flow reactor

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