Determination of phenol concentrations by an electrochemical system with immobilized tyrosinase

J. G. Schiller; A. K. Chen; C. C. Liu

doi:10.1016/0003-2697(78)90269-5

Determination of phenol concentrations by an electrochemical system with immobilized tyrosinase

J. G. Schiller, A. K. Chen, C. C. Liu

材料科學與工程研究所

研究成果: 雜誌貢獻 › 期刊論文 › 同行評審

46 引文斯高帕斯（Scopus）

摘要

An electrochemical system has been devised to measure phenol concentrations in aqueous solutions. The unit employs the immobilized enzyme, tyrosinase, to oxidize phenol in the presence of saturating levels of oxygen. The oxidation product, ortho-benzoquinone, is then chemically reduced in the presence of an excess of ferrocyanide ions. The coupled oxidation of ferrocyanide ions to ferricyanide ions results in a measurable potential difference in the electrochemical system. The resulting zero current potentials in these steady-state potentiometric measurements are shown to be directly proportional to the logarithm of phenol concentration over the range of 3.8 × 10^-7 to 1 × 10^-4 m. The results of studies carried out with alternate substrates for the enzyme and interfering compounds are also presented.

原文	???core.languages.en_GB???
頁（從 - 到）	25-33
頁數	9
期刊	Analytical Biochemistry
卷	85
發行號	1
DOIs	https://doi.org/10.1016/0003-2697(78)90269-5
出版狀態	已出版 - 3月 1978

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10.1016/0003-2697(78)90269-5

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title = "Determination of phenol concentrations by an electrochemical system with immobilized tyrosinase",

abstract = "An electrochemical system has been devised to measure phenol concentrations in aqueous solutions. The unit employs the immobilized enzyme, tyrosinase, to oxidize phenol in the presence of saturating levels of oxygen. The oxidation product, ortho-benzoquinone, is then chemically reduced in the presence of an excess of ferrocyanide ions. The coupled oxidation of ferrocyanide ions to ferricyanide ions results in a measurable potential difference in the electrochemical system. The resulting zero current potentials in these steady-state potentiometric measurements are shown to be directly proportional to the logarithm of phenol concentration over the range of 3.8 × 10-7 to 1 × 10-4 m. The results of studies carried out with alternate substrates for the enzyme and interfering compounds are also presented.",

author = "Schiller, {J. G.} and Chen, {A. K.} and Liu, {C. C.}",

note = "Funding Information: The technical assistance of Edna Klatt and Vera Londino on this work is appreciated. Also, the support of this work by the Lewis Research Center, NASA, under Research Grant NSG-3002 is gratefully acknowledged. The discussions and comments by Dr. J. Stuart Fordyce of the Lewis Research Center are also appreciated.",

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AU - Schiller, J. G.

AU - Chen, A. K.

AU - Liu, C. C.

N1 - Funding Information: The technical assistance of Edna Klatt and Vera Londino on this work is appreciated. Also, the support of this work by the Lewis Research Center, NASA, under Research Grant NSG-3002 is gratefully acknowledged. The discussions and comments by Dr. J. Stuart Fordyce of the Lewis Research Center are also appreciated.

PY - 1978/3

Y1 - 1978/3

N2 - An electrochemical system has been devised to measure phenol concentrations in aqueous solutions. The unit employs the immobilized enzyme, tyrosinase, to oxidize phenol in the presence of saturating levels of oxygen. The oxidation product, ortho-benzoquinone, is then chemically reduced in the presence of an excess of ferrocyanide ions. The coupled oxidation of ferrocyanide ions to ferricyanide ions results in a measurable potential difference in the electrochemical system. The resulting zero current potentials in these steady-state potentiometric measurements are shown to be directly proportional to the logarithm of phenol concentration over the range of 3.8 × 10-7 to 1 × 10-4 m. The results of studies carried out with alternate substrates for the enzyme and interfering compounds are also presented.

AB - An electrochemical system has been devised to measure phenol concentrations in aqueous solutions. The unit employs the immobilized enzyme, tyrosinase, to oxidize phenol in the presence of saturating levels of oxygen. The oxidation product, ortho-benzoquinone, is then chemically reduced in the presence of an excess of ferrocyanide ions. The coupled oxidation of ferrocyanide ions to ferricyanide ions results in a measurable potential difference in the electrochemical system. The resulting zero current potentials in these steady-state potentiometric measurements are shown to be directly proportional to the logarithm of phenol concentration over the range of 3.8 × 10-7 to 1 × 10-4 m. The results of studies carried out with alternate substrates for the enzyme and interfering compounds are also presented.

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Determination of phenol concentrations by an electrochemical system with immobilized tyrosinase

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