Vorob'eva L I, Al-Sudant S, Kraeva N I
Mikrobiologiia. 1986 Sep-Oct;55(5):750-3.
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.
在谢氏丙酸杆菌中发现了过氧化物酶活性。已开发出分离和纯化该酶的方法。结果表明它是一种含血红素的蛋白质，对过氧化氢具有特异性，在20至30摄氏度下稳定，在pH 6.8至7.0时发挥最佳作用。研究了酶催化反应速率与酶和底物浓度的函数关系。测定了过氧化氢和邻联茴香胺的米氏常数（Km）。
