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Updated: May 29, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Influence of stabilizers cosolutes on catalase conformation
Soledad Belluzo1, Valeria Boeris, Beatriz Farruggia
1Lab. of Physical Chemistry Applied to the Bioseparation, Faculty of Biochemical and Pharmaceutical Sciences, CONICET, National University of Rosario, (S2002RLK) Rosario, Argentina. sbelluzo@fbioyf.unr.edu.ar
Abstract:
The effects of sucrose, mannitol and betaine on the thermodynamic stability and the conformational state of the catalase enzyme were analyzed in order to understand the molecular mechanism whereby the solutes stabilized the enzyme. Catalase was selected as the model enzyme because it is used in several biotechnological processes. In the presence of each cosolute, our data have shown that there was a significant increase in the thermal stability of catalase. A minor stabilization in the enzyme secondary structure were induced by these cosolutes, as circular dichroism in the far UV region has demonstrated. Furthermore, our results support the idea that the overall native structure of catalase becomes more rigid, at least in certain surface areas, in the presence of the assayed stabilizers. This last finding can be reasonably explained by the exclusion mechanism of cosolutes from the protein surface which increases the structured water around this area.
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