Intrinsic fluorescence of enzymes and fluorescence of chemically modified enzymes for analytical purposes: a review.
In recent years our research group has developed new alternatives for fluorescence enzymatic determinations. First, we observed that the intrinsic fluorescence of enzymes changes during enzymatic reactions, proportionally to the substrate concentration, avoiding the combination of the enzymatic reaction with a fluorophore-involving reaction. The main disadvantage of this method is that the excitation and emission wavelengths of the enzymes are in the UV region of the spectrum. An alternative to overcome this problem consisted of covalently bonding the enzyme to a fluorophore. In this paper, an overview is given of all of the applications and future developments on both types of alternatives that we have developed. Apart from the analytical characteristics of the methods, we have also reviewed all of the information about mathematical models we have elaborated to date.
Galbán
J
J
Analytical Spectroscopy and Sensors Group (GEAS), Department of Analytical Chemistry, Faculty of Sciences, University of Zaragoza, -E-50009 Zaragoza, Spain. jgalban@posta.unizar.es
Andreu
Y
Y
Sierra
J F
JF
de Marcos
S
S
Castillo
J R
JR
D004798:Enzymes / Q000737:chemistry*; D005453:Fluorescence; D013056:Spectrophotometry, Ultraviolet
D004798:Enzymes