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Updated: Aug 7, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
Pharmacokinetics and stability properties of catalase modified with water-soluble polysaccharides
Aymara Valdivia1, Yunel Pérez, Leissy Gómez
1Center for Enzyme Technology, University of Matanzas, Matanzas, Cuba.
Abstract:
Bovine liver catalase (EC 1.11.1.6) was chemically modified with mannan, carboxymethylcellulose, and carboxymethylchitin. The enzyme retained about 48-97% of the initial specific activity after glycosidation with the polysaccharides. The prepared neoglycoenzyme was 1.9-5.7 fold more stable against the thermal inactivation processes at 55 degrees C, in comparison with the native counterpart. Also, the modified enzyme was more resistant to proteolytic degradation with trypsin. Pharmacokinetics studies revealed higher plasma half-life time for all the enzyme-polymer preparations, but better results were achieved for the enzyme modified with the anionic macromolecules.
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