1970 Volume 17 Issue 10 Pages 443-446
The catalytic properties of crude sweet potato peroxidase preparation was investigated in comparison with those of horseradish peroxidase.
Sulfite, indoleacetate and oxaloacetate were oxidatively catalyzed with both enzymes, in the presence of Mn++ and a monophenol, such as 2, 4-dichlorophenol. Sulfite oxidative activity in crude sweet potato peroxidase preparation was different from that of horseradish peroxidase.
When sweet potato tissue slices were incubated in ethylene (10ppm) containing air, both peroxidase and oxidase activities increased in the slices, and the ratio of oxidative activity to peroxidative activity was found to be gradually increased 24 hours after incubation.