[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 (8.4 kDa) compared with the native enzyme.
Artiukhov
V G
VG
Kovaleva
T A
TA
Kholiavka
M G
MG
Bitiutskaia
L A
LA
Grechkina
M V
MV
Obraztsova
T B
TB
D005656:Fungal Proteins / Q000737:chemistry*; D006026:Glycoside Hydrolases / Q000737:chemistry*; D007716:Kluyveromyces / Q000201:enzymology*; D011487:Protein Conformation; D055503:Protein Multimerization; D021122:Protein Subunits / Q000737:chemistry
D005656:Fungal Proteins; D021122:Protein Subunits; D006026:Glycoside Hydrolases; C023086:inulinase