Park K H, Fricker A
Z Lebensm Unters Forsch. 1977 Jul 29;164(3):167-70. doi: 10.1007/BF01263024.
The thermal reaction of the two components of the horseradish peroxidase--the apoenzyme and the prosthetic group--with that of the holoenzyme were compared. From this we conclude that the thermal inactivation of the peroxidase in aqueous solution is not caused by a change of the apoprotein alone, but rather by participation of the entire three-dimensional structure including the prosthetic group. Spectrophotometric studies of the inactivation process in the holoenzyme revealed that the absorbance of the Soret band changes parallely to a reduction of the enzyme activity during heating. Since it has been found that the Soret absorption increases again during storage and simultaneously the enzyme activity regenerates, the change of the Soret absorption during heating can be regarded as the result of both reversible and irreversible denaturation processes.
