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Diphenolases from Anoxybacillus kestanbolensis strains K1 and K4 T

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Summary

Diphenolases from Anoxybacillus kestanbolensis strains K1 and K4T, highly active against 4-methylcatechol were characterized in terms of pH- and temperature-optima, pH- and temperature-stability, kinetic parameters, and inhibition/activation behaviour towards some general polyphenol oxidase (PPO) inhibitors and metal ions. The temperature-activity optima, for Anoxybacillus kestanbolensis K1 and K4T catecholases in the presence of 4-methylcatechol, were 80 and 70 °C, respectively. Although catecholase from A. kestanbolensis K4T lost no activity after a period of 1 h incubation at its optimum temperature, the enzyme pH from K1 was stimulated by keeping at 80 °C. Both of the enzymes possessed pH optima at 9.5, and the pH-stability profiles showed that cathecholases from both preparations retained their activities at alkaline pH values. Both A. kestanbolensis K1 and K4T catecholase activities were totally inhibited by addition of 0.01 mM sodium metabisulphite, ascorbic acid and l-cysteine. 1 mM Mn2+ increased the activities of A. kestanbolensis K1 and K4T catecholases by 6.4- and 5.3-fold, respectively. These results indicate that both A. kestanbolensis K1 and K4T strains possess thermo- and alkalostable catecholases.

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Authors and Affiliations

  1. Departments of Chemistry, Karadeniz Technical University, 61080, Trabzon, Turkey

    Melike Yildirim, Melek Col, Ahmet Colak & Saadettin Güner

  2. Department of Biology, Karadeniz Technical University, 61080, Trabzon, Turkey

    Ali Osman Beldüz

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  1. Melike Yildirim
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  2. Melek Col
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  3. Ahmet Colak
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  4. Saadettin Güner
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  5. Sabriye Dülger
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  6. Ali Osman Beldüz
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Correspondence to Melike Yildirim.

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Yildirim, M., Col, M., Colak, A. et al. Diphenolases from Anoxybacillus kestanbolensis strains K1 and K4 T. World J Microbiol Biotechnol 21, 501–507 (2005). https://doi.org/10.1007/s11274-004-2392-0

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