Abstract
The conditions and mechanisms of the immobilization of inulinase on polymeric carriers were studied using the VION KN-1 and KU-2 cation-exchangers, VION AN-1 and AV-17-2P anion-exchangers, and the ampholyte KOPAN-90. The calculated data showed a significant role of van der Waals interactions and hydrogen bonding in the formation of virtually all inulinase complexes with the immobilization matrices. The AV-17-2P anion-exchanger was the only one of the studied polymer matrices that was unable to form hydrogen bonds with inulinase. The mechanisms of the interaction between inulinase and various ampholytes and cation and anion exchange resins differ from each other. The strongest differences are observed in mechanisms of the sorption of inulinase on VION KN-1 and chitosan matrices. Approximately 87% of the identical amino-acid residues are involved in the interaction of the enzyme with the KU-2 and AV-17-2P resins and the VION AN-1 and KOPAN-90 fibers.
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Original Russian Text © M.G. Holyavka, M.S. Kondratyev, V.V. Terentyev, A.A. Samchenko, A.V. Kabanov, V.M. Komarov, V.G. Artyukhov, 2017, published in Biofizika, 2017, Vol. 62, No. 1, pp. 9–16.
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Holyavka, M.G., Kondratyev, M.S., Terentyev, V.V. et al. The molecular mechanism of adsorption immobilization of inulinase on polymer matrices. BIOPHYSICS 62, 5–11 (2017). https://doi.org/10.1134/S0006350917010109
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DOI: https://doi.org/10.1134/S0006350917010109