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- W2079411967 abstract "A thermostable catalase from the culture broth of Thermoascus aurantiacus grown on ethanol was purified as an electrophoretically and isoelectrophoretically homogeneous protein. The molecular weights of the native enzyme and its subunit were estimated to be approximately 330,000 and 75,000 by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis, respectively. The enzyme was proven to be a homo-tetrameric hemecatalase with one iron atom per subunit and about 11% carbohydrate. The pI was 4.5. The enzyme was stable up to 80°C and over a wide range of pH from 5 to 13. The optimum pH was in the range of 6 to 10 and the optimum temperature was 70°C. The Km and Kcat of the enzyme for hydrogen peroxide were 4.8 × 10−2 M and 1.07 × 105s−1, respectively. The enzyme was strongly inhibited by potassium cyanide and sodium azide." @default.
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- W2079411967 date "1998-01-01" @default.
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- W2079411967 title "Purification and characterization of a thermostable catalase from culture broth of Thermoascus aurantiacus" @default.
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- W2079411967 doi "https://doi.org/10.1016/s0922-338x(97)86762-1" @default.
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