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Activation by organic solvents of an alkaline thermostable peroxidase partially purified from rice hulls

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Abstract

A thermostable alkaline peroxidase was partially purified from rice hulls by precipitation in 70% (v/v) isopropanol, anion exchange chromatography on a DEAE cellulose column (eluted by 50 mM potassium phosphate, pH 6.0), and gel filtration on a Sephacryl S-200 column. The peroxidase (RHP) showed a maximum activity at a slightly alkaline condition, between pH 7 and 8, for the oxidation of guaiacol in the presence of 0.2 mM H O . The half life time for the inactivation of RHP at 68°C was 168 min nearly six times that of horseradish peroxidase (HRP) at the same temperature. Dioxane enhanced the activity of RHP but decreased that of HRP.

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Authors and Affiliations

  1. Department of Chemical Engineering, The University of Ulsan, Ulsan, 680-749, Korea

    K. Ryu & Y. Kim

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  1. K. Ryu
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  2. Y. Kim
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Ryu, K., Kim, Y. Activation by organic solvents of an alkaline thermostable peroxidase partially purified from rice hulls. Biotechnology Letters 19, 1019–1022 (1997). https://doi.org/10.1023/A:1018455502834

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  • DOI: https://doi.org/10.1023/A:1018455502834

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