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The intracellular bacterial peroxidase from Pseudomonas sp. SUK1 was purified by anion exchange and molecular sieve chromatography. The molecular weight of the purified peroxidase was estimated to be 86 kDa by SDS-PAGE analysis. The UV-visible absorption spectra revealed that the purified peroxidase was a heme-containing protein. The purified enzyme exerted its optimal activity with n-propanol and...
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