Effect of compatible and noncompatible osmolytes on the enzymatic activity and thermal stability of bovine liver catalase

• Published in: Journal of biomolecular structure & dynamics 2013-12, Vol.31 (12), p.1440-1454
• Main Authors: Sepasi Tehrani, H., Moosavi-Movahedi, A.A., Ghourchian, H., Ahmad, F., Kiany, A., Atri, M.S., Ariaeenejad, Sh, Kavousi, K., Saboury, A.A.
• Format: Article
• Language: English
• Subjects: Animals; Biocatalysis - drug effects; catalase; Catalase - chemistry; Catalase - metabolism; Cattle; chemometrics; Circular Dichroism; Enzyme Stability - drug effects; functional stability; histidine; Histidine - chemistry; Histidine - metabolism; Histidine - pharmacology; Hydrogen Peroxide - metabolism; Kinetics; Liver - enzymology; Models, Molecular; Molecular Structure; osmolytes; proline; Proline - chemistry; Proline - metabolism; Proline - pharmacology; Protein Binding; Protein Denaturation - drug effects; Protein Structure, Tertiary; Spectrophotometry; Temperature; thermal stability; Transition Temperature - drug effects; Valine - chemistry; Valine - metabolism; Valine - pharmacology; Xylitol - chemistry; Xylitol - metabolism; Xylitol - pharmacology
• ISSN: 0739-1102; 1538-0254
• DOI: 10.1080/07391102.2012.742460

Catalase is an important antioxidant enzyme that catalyzes the disproportionation of H 2 O 2 into harmless water and molecular oxygen. Due to various applications of the enzyme in different sectors of industry as well as medicine, the enhancement of stability of the enzyme is important. Effect of various classes of compatible as well as noncompatible osmolytes on the enzymatic activity, disaggregation, and thermal stability of bovine liver catalase have been investigated. Compatible osmolytes, proline, xylitol, and valine destabilize the denatured form of the enzyme and, therefore, increase its disaggregation and thermal stability. The increase in the thermal stability is accompanied with a slight increase of activity in comparison to the native enzyme at 25 °C. On the other hand, histidine, a noncompatible osmolyte stabilizes the denatured form of the protein and hence causes an overall decrease in the thermal stability and enzymatic activity of the enzyme. Chemometric results have confirmed the experimental results and have provided insight into the distribution and number of mole fraction components for the intermediates. The increase in melting temperature (T m ) and enzymatic rate could be further amplified by the intrinsic effect of temperature enhancement on the enzymatic activity for the industrial purposes.