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Isolation and Study of Some Properties of Laccase from the Basidiomycetes Cerrena maxima

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Abstract

A new strain producing extracellular laccase (Cerrena maxima 0275) was found by screening of isolates of Basidiomycetes, and the dynamics of laccase biosynthesis by this strain was studied. The enzyme was purified to homogeneity. The molecular weight of the enzyme is 57 kD, and its pI is 3.5. The activity is constant at pH values in the range 3.0-5.0. The temperature optimum for activity is 50°C. The thermal stability of the laccase was studied. The catalytic and Michaelis constants for catechol, hydroquinone, sinapinic acid, and K4 Fe(CN)6 were determined. The standard redox potential of type 1 copper in the enzyme is 750 ± 5 mV. Thus, the investigated laccase is a high redox potential laccase.

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Authors and Affiliations

  1. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow, 117071, Russia

    O. V. Koroleva, I. S. Yavmetdinov, S. V. Shleev & E. V. Stepanova

  2. Komarov Botanical Institute, Russian Academy of Sciences, ul. Prof. Popova 2, St. Petersburg, 197022, Russia

    V. P. Gavrilova

Authors
  1. O. V. Koroleva
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  2. V. P. Gavrilova
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  3. I. S. Yavmetdinov
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  4. S. V. Shleev
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  5. E. V. Stepanova
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Koroleva, O.V., Gavrilova, V.P., Yavmetdinov, I.S. et al. Isolation and Study of Some Properties of Laccase from the Basidiomycetes Cerrena maxima. Biochemistry (Moscow) 66, 618–622 (2001). https://doi.org/10.1023/A:1010299012591

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