Affiliation:
1. M.V. Lomonosov Moscow State University; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences
2. N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences
3. M.V. Lomonosov Moscow State University
Abstract
The paper addresses the possibilities of voltammetry, surface-enhanced Raman spectroscopy (SERS) and mass spectrometry in tandem with enzymatic catalysis. The basic principles of operation of electrochemical biosensors based on oxidases and dehydrogenases are described. It has been shown that biosensors using cyclic enzymatic reactions and substrate recycling have the best sensitivity. The variants of significant improvement of the analytical potential of biosensor analysis due to the use of polymers for effective modification of the electrode surface and non-destructive immobilization of enzymes are illustrated. The data demonstrating how the use of enzyme labels expands the range of bioanalytical applications of SERS are presented. The possibility of highly sensitive measurement of the activity of enzyme labels (peroxidase, alkaline phosphatase, β-galactosidase) using SERS, in fact, opens up a new universal platform for the development of methods for the determination of various antigens. By way of example of the most commonly used proteases, the main trends in the development of the methodology of proteomic studies by mass spectrometry, as well as the role of proteases in the design of mass spectrometric experiments, are considered.
Funder
Russian Science Foundation
Reference128 articles.
1. Berezin I.V., Klesov A.A. Enzymes – chemical catalysts? Moscow, 1971. p. 48.
2. Thevenot D.R., Toth K., Durst R.A., Wilson G.S. // Pure Appl. Chem. 1999. Vol. 71. P. 2333.
3. Singh A., Sharma A., Ahmed A., Sundramoorthy A.K., Furukawa H., Arya S., Khosla A. // Biosensors 2021. Vol. 11. P. 336.
4. Clark L.C., Jr., Lyons C. // Ann. N.Y. Acad. Sci. 1962. Vol. 102. P. 29.
5. Gorton L., Lindgren A., Larsson T., Munteanu F.D., Ruzgas T., Gazaryan I. // Anal. Chim. Acta. 1999. Vol. 400. P. 91.