[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.
Artiukhov
V G
VG
Kovaleva
T A
TA
Kholiavka
M G
MG
Bitiutskaia
L A
LA
Grechkina
M V
MV
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
D004800:Enzymes, Immobilized; D007475:Ion Exchange Resins; D019016:Mineral Fibers; D006026:Glycoside Hydrolases; C023086:inulinase