Abstract
Efficiencies of binding between horseradish peroxidase (HRP) and its polymers (HRPp) with inorganic adsorbents (precipitated and coprecipitated) were studied. In aqueous solutions, HRP efficiently adsorbed on aluminum oxide and the coprecipitated sorbent (composed of calcium orthophosphate, magnesium hydroxide, and aluminum hydroxide). HRP readily bound to zinc hydroxide but not to aluminum hydroxide in 25.0 mM bicarbonate buffer (pH 9.0). Several variants of HRP polymerization and HRPp modification with diamines in the presence of Al2O3 and Zn(OH)2 were compared. Synthesis of HRPp according to the scheme comprising HRP activation in solution followed by its polymerization in the presence of Zn(OH)2 appeared the most efficient. HRP and HRPp bound to Zn(OH)2 displayed a high catalytic activity in the presence of high H2O2 concentrations.
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Abbreviations
- BCB:
-
bicarbonate buffer pH 9.0
- HRP:
-
horseradish peroxidase
- HRP*:
-
horseradish peroxidase activated with sodium metaperiodate
- HRPp:
-
horseradish peroxidase polymers
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Translated from Prikladnaya Biokhimiya i Mikrobiologiya, Vol. 41, No. 4, 2005, pp. 383–391.
Original Russian Text Copyright © 2005 by Eryomin, Makarenko, Budnikova.
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Eryomin, A.N., Makarenko, M.V. & Budnikova, L.P. Polymerization of Horseradish Peroxidase in the Presence of Inorganic Adsorbents. Appl Biochem Microbiol 41, 336–343 (2005). https://doi.org/10.1007/s10438-005-0057-x
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DOI: https://doi.org/10.1007/s10438-005-0057-x