[Peroxidase of propionic acid bacteria].
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.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003962:Dianisidine / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D010084:Oxidation-Reduction; D009195:Peroxidase; D010544:Peroxidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D011424:Propionibacterium / Q000201:enzymology*
D007527:Isoenzymes; D006861:Hydrogen Peroxide; D010544:Peroxidases; D009195:Peroxidase; D003962:Dianisidine
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