Adsorption immobilization of inulinase from Aspergillus ficuum and Kluyveromyces marxianus: a comparative aspect
Abstract
Virtual screening of ligands for the immobilization of fungal inulinase from Aspergillus ficuum and yeast inulinase from Kluyveromyces marxianus was performed using computer simulation methods. An algorithm has been developed to reveal the molecular mechanism of adsorption immobilization of inulinases using sequential (cascade) docking methods. The probable binding sites of polymeric matrices with enzyme molecules from various producers were visualized during adsorption immobilization. It has been established that the complexation of inulinase with charged carrier matrices occurs mainly due to hydrogen bonds and van der Waals interactions. It has been shown that during the sorption of inulinases from Aspergillus ficuum and Kluyveromyces marxianus on the matrices KU-2, AV-17-2P, VION KN-1, VION AN-1, KOPAN-90 and chitosan, the following similarities are revealed: 1) when both types of inulinases interact with the KU-2 matrix, hydrogen bonds are formed only between the carrier sulfo groups and the protein molecule; 2) only van der Waals interactions and the absence of hydrogen bonds are revealed between the matrix of the anion exchange resin AV-17-2P and enzymes; 3) chitosan forms the largest number of hydrogen bonds with both inulinases among the carriers studied by us.
Distinctive features of inulinases from Aspergillus ficuum and Kluyveromyces marxianus during sorption on KU-2, AV-17-2P, VION KN-1, VION AN-1, and KOPAN-90 matrices were revealed: 1) binding affinity of yeast inulinase to the surface of KU-2 resin generally higher, and the number of hydrogen bonds and the number of amino acid residues that form van der Waals interactions, is greater than that of the fungal enzyme; 2) the binding affinities and the number of amino acids involved in van der Waals interactions for inulinase from Kluyveromyces marxianus during sorption on the anion exchange resin AV-17-2P also exceed their values for the enzyme from Aspergillus ficuum; 3) in contrast to fungal inulinase, in which 21 amino acid residues are part of the binding sites with all the carriers we studied, the yeast enzyme has only one such residue.
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