Biopolym. Cell. 2000; 16(6):505-509.
Structure and Function of Biopolymers
Catalytic properties of the Penicilium vitate catalase. Peroxidatic reaction of the enzyme
- 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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