Use of catalase from Escherichia coli in model experiments for oxygen supply of microorganisms with hydrogen peroxide.
A catalase has been purified from aerobically grown Escherichia coli K12. The enzyme exhibits unorthodox properties compared with catalyse from bovine liver and seems to be identical to hydroperoxidase II from E. coli. A mathematical model is presented which makes it possible to calculate the steady-state concentration of hydrogen peroxide in an open system. The model has been verified experimentally. It has been shown that the catalase from E. coli is better suited than the bovine liver enzyme for oxygen supply to cell suspensions using hydrogen peroxide.
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Institut für Mikrobiologie der Universität Göttingen, D-3400 Göttingen, Federal Republic of Germany.
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