[Effect of chemical modification on thermal stability of horseradish peroxidase].
Soluble preparations of horse radish peroxidase are obtained by means of its amino groups modification with glutaric aldehyde, maleic anhydride and inert proteins including albumin. The enzyme activity is found to decrease under the modification with glutaric aldehyde and to be unchanged at all other cases. Thermal stability of the enzyme preparations obtained is studied within the temperature range from 56 to 80 degrees C. Thermostability of glutaric aldehyde-modified peroxidase is approximately 2.5-fold decreased at 56 degrees C. Thermostability of other preparations exceeds the stability of native peroxidase in 25--90 times at 56 degrees C. Thermodynamic parameters of activation for the process of irreversible thermoinactivation of native and modified enzyme are calculated. A strong compensation effect between activation enthalpy and entropy values is observed, which were changed in 1.5--2 times, while the free activation energy is changed by 2--3 kcal/mol only. Possible mechanism of the change of the enzyme thermal stability under its chemical modification is discussed.
D055598:Chemical Phenomena; D002621:Chemistry; D004355:Drug Stability; D004789:Enzyme Activation; D005976:Glutaral; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006358:Hot Temperature; D008299:Maleic Anhydrides; D010544:Peroxidases / Q000378:metabolism*; D013816:Thermodynamics
D008299:Maleic Anhydrides; D006735:Horseradish Peroxidase; D010544:Peroxidases; D005976:Glutaral
Vliianie khimicheskoĭ modifikatsii na termicheskuiu stabil'nost' peroksidazy iz khrena.