In this review we explore the advantages deriving from the use of either enzymes or sugar binding proteins isolated from thermophilic organisms to develop stable fluorescence biosensors. We report on a novel approach to address the consumption of the analyte by enzyme-based biosensors, namely the utilization of apo-enzymes as non-active forms of proteins which are still able to bind the ligand but cannot transform it into product. We also report recent studies in which the fluorescence labeling of a naturally thermostable binding protein allows a quantitative determination of glucose.

Thermostable proteins as probe for the design of advanced fluorescence biosensors.

Staiano M;Aurilia V;Parracino A;Rossi M;
2006

Abstract

In this review we explore the advantages deriving from the use of either enzymes or sugar binding proteins isolated from thermophilic organisms to develop stable fluorescence biosensors. We report on a novel approach to address the consumption of the analyte by enzyme-based biosensors, namely the utilization of apo-enzymes as non-active forms of proteins which are still able to bind the ligand but cannot transform it into product. We also report recent studies in which the fluorescence labeling of a naturally thermostable binding protein allows a quantitative determination of glucose.
2006
Istituto di Biochimica delle Proteine - IBP - Sede Napoli
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/125650
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