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Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
Аннотация:The peroxidase activity was found in Propionibacterium shermanii. Methods were developed to isolate and purify the enzyme. It was shown to be a heme-containing protein, specific to H2O2, stable at 20 to 30 degrees C and exerting the optimal action at pH 6.8 to 7.0. The rate of the enzyme-catalysed reaction was studied as a function of the enzyme and substrate concentrations. The Km was determined for H2O2 and o-dianisidine.