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Updated: Jul 9, 2026

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
Published on: April 4, 2014
Sequential conversion by catalytically active MIP and immobilized tyrosinase in a thermistor
K Lettau1, M Katterle, A Warsinke
1University of Potsdam, Analytical Biochemistry, Karl-Liebknecht-Str 24-25, Potsdam-Golm, Germany.
Abstract:
To amplify the heat-signal generated by MIP catalyzed solvolysis of phenylacetate the reaction has been combined for the first time in a reactor with the subsequent oxidation by immobilized tyrosinase. The polymer cleaves the substrate and the released phenol is afterwards converted to o-benzoquinone by the tyrosinase. The separated and sequentially coupled reactions are characterized by the heat generated in a thermistor. The sequential substrate conversion results in a combined heat generation which results a five times higher signal than compared to the polymer alone.

