title: [Purification and properties of inulinases from Aspergillus niger M89].
abstract: Four inulinase components were purified from Aspergillus niger M89 by (NH4)2SO4 fractionation, Sephadex G-200 gel filtration, DEAE-cellulose chromatography and polyacrylamide gel electrophoresis (PAGE). The molecular weight of EI EII EIII and EIV were indicated to be 102.6, 97.9, 62.5 and 36.5 kD respectively by SDS-PAGE. Measured by isoeleetric focusing, their isoelectric points were 4.15, 4.24, 4.48 and 4.15 respectively. Four forms of inulinase exibited maximal inulinase activity between 55-60 degrees C with optimal pH 4.0-5.0. There were some difference in their thermal stability. The little the molecule of the component was, the stronger its thermal stability was. All of four components were exo-acting inulinases.
authors.affiliation: Department of Food Science, Hebei Agricultural University, Baoding 071001.
authors.forename: Y
authors.initials: Y
authors.lastname: Ji
authors.forename: X
authors.initials: X
authors.lastname: Zhao
mesh_terms: D001234:Aspergillus niger / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013696:Temperature
chemical_list: D006026:Glycoside Hydrolases; C023086:inulinase