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Updated: Jul 27, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Thermal stability of catalases active in dormant saffron (Crocus sativus L.) corms
J Keyhani1, E Keyhani, J Kamali
1Laboratory for Life Sciences, Saadat Abade, Tehran, Iran. keyhanie@ibb.ut.ac.ir
Abstract:
Catalase activity was detected in crude extract prepared from dormant saffron (Crocus sativus L.) corms. The activity was independent of pH in the range 6.0-11.0. Thermostability studies suggested the presence of three isoenzymes with transition temperatures of 30 degrees C, 45 degrees C and 60 degrees C, respectively, as given by Arrhenius plots. When stained for catalase activity gel electropherograms of extract revealed 3 distinct bands with apparent molecular weight of 323,000, 295,000 and 268,000, respectively. Thus it appeared that at least three isoenzymes of catalase were present in dormant saffron corms.
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