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Study of the oligomeric structure and some physicochemical properties of inulinase from Kluyveromyces marxianus Y-303

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Abstract

It has been found using a combination of atomic force microscopy with infrared spectroscopy, gel chromatography, and electrophoresis that inulinase from Kluyveromyces marxianus Y-303 has oligomeric structure, which includes two subunits differing in size, molecular mass, and catalytic activity. It has been shown that the division of the inulinase dimer into monomers leads to an increase in the number of irregular regions by 6% for subunit 1 (54.8 kDa) and by 10% for subunit 2 (8.4 kDa) compared with the native enzyme.

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Authors and Affiliations

  1. Voronezh State University, Voronezh, 394006, Russia

    V. G. Artyukhov, T. A. Kovaleva, M. G. Kholyavka, L. A. Bityutskaya, M. V. Grechkina & T. B. Obraztsova

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  1. V. G. Artyukhov
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  2. T. A. Kovaleva
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  3. M. G. Kholyavka
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  4. L. A. Bityutskaya
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  5. M. V. Grechkina
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  6. T. B. Obraztsova
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Corresponding author

Correspondence to T. A. Kovaleva.

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Original Russian Text © V.G. Artyukhov, T.A. Kovaleva, M.G. Kholyavka, L.A. Bityutskaya, M.V. Grechkina, T.B. Obraztsova, 2009, published in Biofizika, 2009, Vol. 54, No. 6, pp. 1005–1011.

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Artyukhov, V.G., Kovaleva, T.A., Kholyavka, M.G. et al. Study of the oligomeric structure and some physicochemical properties of inulinase from Kluyveromyces marxianus Y-303. BIOPHYSICS 54, 675–680 (2009). https://doi.org/10.1134/S0006350909060025

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  • DOI: https://doi.org/10.1134/S0006350909060025

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