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.
CITATION STYLE
De Champdoré, M., Staiano, M., Aurilia, V., Stepanenko, O. V., Parracino, A., Rossi, M., & D’Auria, S. (2007). Thermostable proteins as probe for the design of advanced fluorescence biosensors. In Life in Extreme Environments (Vol. 9781402062858, pp. 45–54). Springer Netherlands. https://doi.org/10.1007/978-1-4020-6285-8_3
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