Voronezh, Voronezh, Russian Federation
We study the conditions and mechanisms of immobilization of inulinase with immobilization carriers (fragments of matrices of ion-exchanger KU-2 and AV-17-2P) and find their binding affinities. The calculated data show a significant role played by van der Waals interaction and hydrogen bonds in forming complexes of inulinase with a matrix of KU-2 resin, while AV-17-2P doesn't form hydrogen binding with inulinase, but forms only van der Waals interaction. It is established that, despite considerable coincidence of the amino acid in contact area of enzyme-carrier complex (which constitutes 60% of total number of the amino acids participating in the immobilization bond for KU-2 and 47% for AV-17-2P), mechanisms of adsorption of inulinase on positive and negatively charged ligand matrices significantly differ from each other.
computer modeling, inulinase, immobilization, molecular docking, KU-2, AV-17-2P
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