title: [Thermal inactivation of free and immobilized inulinase].
abstract: 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.
authors.forename: V G
authors.initials: VG
authors.lastname: Artiukhov
authors.forename: T A
authors.initials: TA
authors.lastname: Kovaleva
authors.forename: M G
authors.initials: MG
authors.lastname: Kholiavka
authors.forename: L A
authors.initials: LA
authors.lastname: Bitiutskaia
authors.forename: M V
authors.initials: MV
authors.lastname: Grechkina
mesh_terms: D000327:Adsorption; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D006358:Hot Temperature; D007475:Ion Exchange Resins / Q000737:chemistry; D007716:Kluyveromyces / Q000201:enzymology*; D019016:Mineral Fibers; D013997:Time Factors
chemical_list: D004800:Enzymes, Immobilized; D007475:Ion Exchange Resins; D019016:Mineral Fibers; D006026:Glycoside Hydrolases; C023086:inulinase