Abstract
Two methods were used to separate heme and apoenzyme from the holoenzyme of peroxidase (EC 1.11.1.7) isolated from medium of cultured peanut cells. Apoenzyme prepared by either method lacked peroxidase activity but possessed indole acetic acid (IAA) oxidase and poly phenol oxidase (PPO) (EC 1.14.18.1) activity. When the holoenzyme was reconstituted with heme and apoenzyme, peroxidase activity was restored. The studies on the active site revealed that PPO and IAA oxidase share the same active site on the apoenzyme.
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