T.A. Kovaleva, M.G. Holyavka

IR-specters of inulinases from Kluyveromyces marxianus Y-303 and Aspergillus awamori BKMF 2250 are received. Correlation of the second structure types for these proteins is defined. It is showed, that the enzyme from Kluyveromyces marxianus have the more order globule: it has less irregular sectors and more α-helix and β-strand then inulinase from Aspergillus awamori. At the analysis of primary structures of enzymes it is difficultly to determine, what inulinase from the researched proteins will have more rigid molecular conformation, as for inulinase from Kluyveromyces marxianus is characteristic smaller (on 0,43 %) amount of helix-forming and smaller (on 1,54 %) amount of helix-destroying rests of aminoacides in comparison with inulinase from Aspergillus awamori. However the analysis of secondary structures for inulinases from Kluyveromyces marxianus Y-303 and Aspergillus awamori ВКМF 2250 allows us to make the assumption about of greater orderliness for protein globules of yeast origin enzyme, and consequently, about its greater stability to various denaturizing , especially thermal, influences.