Applied Biochemistry and Biotechnology

, Volume 76, Issue 1, pp 45–55 | Cite as

Effect of thermosensitive matrix-phase transition on urease-catalyzed urea hydrolysis

  • Nikolay L. Eremeev
  • Alexandr V. Kukhtin
  • Eugenia A. Belyaeva
  • Novella F. Kazanskaya


Temperature dependencies of kinetic and equilibrium parameters of urea hydrolysis catalyzed by native urease and the urease immobilized in a thermosensitive poly-N-isopropylacrylamide gel have been studied. The swelling ratio of the collapsed urease-containing gel is shown to increase in the presence of urea. Below a lower critical solution temperature (LCST) of the polymer, the immobilized u reaseactually has thesame catalytic properties as the native enzyme. At temperatures above LCST, the observed catalytic activity of the immobilized enzyme depends chiefly not only on the thermoreversible matrix state, but also on gel water content.

Index Entries

Enzymekinetics urease urea hydrolysis thermoreversible hydrogels phase transition enzyme activity thermoregulation 



activation energy, kJ/mol


Michaelis constant, M


reaction rate, mM/min


maximum reaction rate, mM/min


maximum reaction rate in a pH optimum of enzyme activity, mM/min


temperature, K


temperatue, °C


urea concentration, M


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Copyright information

© Humana Press Inc 1999

Authors and Affiliations

  • Nikolay L. Eremeev
    • 1
  • Alexandr V. Kukhtin
    • 1
  • Eugenia A. Belyaeva
    • 1
  • Novella F. Kazanskaya
    • 1
  1. 1.Department of Chemical Enzymology, Faculty of ChemistryLomonosov Moscow State UniversityMoscowRussia

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