Catalatic activity of lactoperoxidase in the presence of SCN-
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Updated: Oct 21, 2026
04:41
Measuring Lactase Enzymatic Activity in the Teaching Lab
Published on: August 6, 2018
Biochemical and Biophysical Research Communications
|October 31, 1983
Abstract:
Lactoperoxidase catalyzed the catalatic decomposition of H2O2 in the presence of SCN-. The pH optimum for O2 evolution was 8.5, while the enzyme activity as disclosed by the rate of H2O2 disappearance was optimal at 4.5. Since the catalatic activity of lactoperoxidase was SCN- dependent, and no O2 was evolved, when H2O2 was added to OSCN- in the absence of lactoperoxidase, an enzyme-OSCN complex may be assumed to be an intermediate in the catalatic activity of lactoperoxidase.
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