Biopolym. Cell. 2000; 16(6):505-509.
Structure and Function of Biopolymers
Catalytic properties of the Penicilium vitate catalase. Peroxidatic reaction of the enzyme
1Latyshko N. V., 1Gudkova L. V., 1Gudkova O. A.
  1. Palladin Institute of Biochemistry, NAS of Ukraine
    9, Leontovycha Str., Kyiv, Ukraine, 01601

Abstract

Peroxidatic activity of the P. vitale catalase with ethanol as a substrate was investigated. It was determined that the peroxidatic activity of the catalase (5–13 U/mg) was over a hundred times less the catalatic activity. Study of the steady-state kinetics showed that kinetic parameters of peroxidatic reaction -Km 5.9 mM and Vmax 0.22 mM/min were lower tlian estimated earlier kinetics of Jlitj catalytic reaction. However, the turnover number kcat -1.1·103 s–1 and catalatic efficiency kM/Km ratio 1.9·105 M s testify the catalase is rather effective peroxidase. The enzyme /fas the rate constant of the peroxidatic action equal to 2.4·104 s–1 M–1 as catalases of other origins.

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