[Inulinases from various producers: the features of their permolecular organization].

The structural organization of inulinases from yeasts, fungi, and plants are researched. For studying their sizes, molecular weight, and permolecular organization, an approach consisting of a combination of atomic force microscopy with methods of dynamic light scattering, gel chromatography, and electrophoresis was used. It is shown that inulinases from Kluyveromyces marxianus and Aspergillus niger form geterodimers and inulinases from tubers of Helianthus tuberosus are present as both dimers and monomers.

[Structural and functional properties of inulinases. Ways to regulate their activity].

The presented review is devoted to the analysis of structural and functional properties of inulinases from various producers. A special attention is given to the questions of molecular and permolecular organization of enzymes, description of their functional features depending upon their structural conditions and in various microenvironment. Perspectives of the development of biotechnological processes with the use of free and immobilized inulinases are discussed from a biophysical viewpoint.

[Thermal inactivation of free and immobilized inulinase].

Thermal inactivation of the Kluyveromyces marxianus inulinase in a free form and immobilized on VION KN-1 cation exchange fiber was studied. Atomic force microscopy demonstrated an oligomeric structure of this enzyme, composed of two subunits differing in their size. It was assumed that the intersubunit contacts were destroyed at 60 degrees C, and the inulinase molecule dissociated into two monomers located separately.

[Oligomeric structure and physicochemical properties of inulinase from Kluyveromyces marxianus Y-303].

It has been found using a combination of atomic force microscopy with infrared spectroscopy, gel chromatography, and electrophoresis that inulinase from Kluyveromyces marxianus Y-303 has oligomeric structure, which includes two subunits differing in size, molecular mass, and catalytic activity. It has been shown that the division of the inulinase dimer into monomers leads to an increase in the number of irregular sites by 6% for subunit 1 (54.8 kDa) and by 10% for subunit 2 (8.