[Effect of temperature on structure and functional properties of horseradish peroxidase].
The dynamics of structural and functional changes proceeding in a peroxidase molecule under the effect of temperature was studied. It was shown that peroxidase thermoinactivation proceeds in two consequent stages. Based on the analysis of enzyme peroxidase and oxidase activity and peroxidase spectral and buffer characteristics, it was established that at temperatures from 20 to 55 degrees C reversible conformation there occur changes of the hemoprotein molecule related to consequent unfolding and folding of the protein globule. The influence of temperature of 60 degrees C and above induces the protein globule unfolding and loosing of peroxidase activity.
Voronezh State University, Russia.
V G
VG
Artiukhov
O V
OV
Basharina
A Iu
AIu
Iskusnykh
D031215:Armoracia / Q000201:enzymology*; D002384:Catalysis; D002850:Chromatography, Gel; D003962:Dianisidine / Q000737:chemistry; D004795:Enzyme Stability; D006735:Horseradish Peroxidase / Q000737:chemistry* / Q000378:metabolism; D006358:Hot Temperature; D007700:Kinetics; D010084:Oxidation-Reduction; D018517:Plant Roots / Q000201:enzymology
D006735:Horseradish Peroxidase; D003962:Dianisidine