Supramolecular Organization of Inulinases from Aspergillus awamori, Aspergillus ficuum and Kluyveromyces marxianus: A Comparative Aspect

Abstract

Computer models for the dimers of inulinases from Aspergillus awamori, Aspergillus ficuum and Kluyveromyces marxianus have been developed. The inulinases dimerization mechanisms from various producers and the amino acid composition of binding sites between the monomers in dimer structure have been studied. Exoinulinase dimers are more similar in structure than endoinulinase dimer. Nonpolar amino acids play the key role in the process of inulinase dimerization during the formation of a bond between the monomer forms of the enzyme from both molds and yeast.