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A multienzyme bioreactor based on a chitinase complex

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Abstract

A heterogeneous biocatalyst containing a complex of chitinolytic enzymes isolated from the culture medium of bacteria Clostridium paraputrificum on the surface of macroporous monolithic minidisc was obtained. The complex of chitinolytic enzymes was immobilized on the polymer matrix using a multistep method involving the introduction of an intermediate macromolecular spacer. The endochitinase and N-acetylglucosaminidase activity of the heterogeneous biocatalyst was studied.

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Authors and Affiliations

  1. Institute of Macromolecular Compounds, Russian Academy of Science, St. Petersburg, 199004, Russia

    E. G. Vlakh, E. A. Ponomareva & T. B. Tennikova

  2. Institute of Chemistry, St. Petersburg State University, St. Petersburg, 198504, Russia

    E. G. Vlakh & T. B. Tennikova

Authors
  1. E. G. Vlakh
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  2. E. A. Ponomareva
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  3. T. B. Tennikova
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Corresponding author

Correspondence to T. B. Tennikova.

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Original Russian Text © E.G. Vlakh, E.A. Ponomareva, T.B. Tennikova, 2014, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2014, Vol. 50, No. 5, pp. 475–480.

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Vlakh, E.G., Ponomareva, E.A. & Tennikova, T.B. A multienzyme bioreactor based on a chitinase complex. Appl Biochem Microbiol 50, 441–446 (2014). https://doi.org/10.1134/S0003683814050123

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  • DOI: https://doi.org/10.1134/S0003683814050123

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