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

Authors: Eremeev, Nikolay¹; Kukhtin, Alexandr²; Belyaeva, Eugenia²; Kazanskaya, Novella²

Source: Applied Biochemistry and Biotechnology, Volume 76, Number 1, February 1999 , pp. 45-55(11)

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Abstract:

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.

Keywords: Enzymekinetics; urease; urea hydrolysis; thermoreversible hydrogels; phase transition; enzyme activity thermoregulation

Document Type: Research article

DOI: http://dx.doi.org/10.1385/ABAB:76:1:45

Affiliations: 1: Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119899, Moscow, Russia, Email: nfk_lab@enzyme.chem.msu.su 2: Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119899, Moscow, Russia,

Publication date: 1999-02-01