A thermophilic apoglucose dehydrogenase as nonconsuming glucose sensor

Sabato D'Auria; Nicolas Di Cesare; Zygmunt Gryczynski; Ignacy Gryczynski; Mosé Rossi; Joseph R. Lakowicz

doi:10.1006/bbrc.2000.3172

A thermophilic apoglucose dehydrogenase as nonconsuming glucose sensor

Sabato D'Auria, Nicolas Di Cesare, Zygmunt Gryczynski, Ignacy Gryczynski, Mosé Rossi, Joseph R. Lakowicz

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Abstract

Blood glucose is a clinically important analytes for diabetic health care. In this preliminary report we describe a protein biosensor for D-glucose based on a thermostable glucose dehydrogenase. The glucose dehydrogenase was noncovalently labeled with 8-anilino-1-naphthalene sulfonic acid (ANS). The ANS-labeled enzyme displayed an approximate 25% decrease in emission intensity upon binding glucose. This decrease can be used to measure the glucose concentration. Our results suggest that enzymes which use glucose as their substrate can be used as reversible and nonconsuming glucose sensors in the absence of required cofactors. Moreover, the possibility of using inactive apoenzymes for a reversible sensor greatly expands the range of proteins which can be used as sensors, not only for glucose, but for a wide variety of biochemically relevant analytes. (C) 2000 Academic Press.

Original language	English
Pages (from-to)	727-731
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	274
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.2000.3172
State	Published - 11 Aug 2000

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title = "A thermophilic apoglucose dehydrogenase as nonconsuming glucose sensor",

abstract = "Blood glucose is a clinically important analytes for diabetic health care. In this preliminary report we describe a protein biosensor for D-glucose based on a thermostable glucose dehydrogenase. The glucose dehydrogenase was noncovalently labeled with 8-anilino-1-naphthalene sulfonic acid (ANS). The ANS-labeled enzyme displayed an approximate 25% decrease in emission intensity upon binding glucose. This decrease can be used to measure the glucose concentration. Our results suggest that enzymes which use glucose as their substrate can be used as reversible and nonconsuming glucose sensors in the absence of required cofactors. Moreover, the possibility of using inactive apoenzymes for a reversible sensor greatly expands the range of proteins which can be used as sensors, not only for glucose, but for a wide variety of biochemically relevant analytes. (C) 2000 Academic Press.",

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AU - D'Auria, Sabato

AU - Di Cesare, Nicolas

AU - Gryczynski, Zygmunt

AU - Gryczynski, Ignacy

AU - Rossi, Mosé

AU - Lakowicz, Joseph R.

N1 - Funding Information: This work was supported by the NIH, National Center for Research Resources, RR-08119.

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Y1 - 2000/8/11

N2 - Blood glucose is a clinically important analytes for diabetic health care. In this preliminary report we describe a protein biosensor for D-glucose based on a thermostable glucose dehydrogenase. The glucose dehydrogenase was noncovalently labeled with 8-anilino-1-naphthalene sulfonic acid (ANS). The ANS-labeled enzyme displayed an approximate 25% decrease in emission intensity upon binding glucose. This decrease can be used to measure the glucose concentration. Our results suggest that enzymes which use glucose as their substrate can be used as reversible and nonconsuming glucose sensors in the absence of required cofactors. Moreover, the possibility of using inactive apoenzymes for a reversible sensor greatly expands the range of proteins which can be used as sensors, not only for glucose, but for a wide variety of biochemically relevant analytes. (C) 2000 Academic Press.

AB - Blood glucose is a clinically important analytes for diabetic health care. In this preliminary report we describe a protein biosensor for D-glucose based on a thermostable glucose dehydrogenase. The glucose dehydrogenase was noncovalently labeled with 8-anilino-1-naphthalene sulfonic acid (ANS). The ANS-labeled enzyme displayed an approximate 25% decrease in emission intensity upon binding glucose. This decrease can be used to measure the glucose concentration. Our results suggest that enzymes which use glucose as their substrate can be used as reversible and nonconsuming glucose sensors in the absence of required cofactors. Moreover, the possibility of using inactive apoenzymes for a reversible sensor greatly expands the range of proteins which can be used as sensors, not only for glucose, but for a wide variety of biochemically relevant analytes. (C) 2000 Academic Press.

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A thermophilic apoglucose dehydrogenase as nonconsuming glucose sensor

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