title: [Immobilization of glucoamylase from Aspergillus awamori 466, and properties of the preparation].
abstract: Glucoamylase from Aspergillus awamori 466 was immobilized on various supports. The enzyme sorption depends on its amount, the type of support, and immobilization conditions. The kinetics of acidic inactivation of the native and immobilized enzyme was studied. The immobilized enzyme was more resistant to temperature and pH. The mechanism of the enzyme binding to the support was investigated by IR spectroscopy.
authors.affiliation: Voronezh State Technological Academy, pr. Revolyutsii 19, Voronezh, 394017 Russia.
authors.forename: I D
authors.initials: ID
authors.lastname: Ruadze
authors.forename: N A
authors.initials: NA
authors.lastname: Zherebtsov
authors.forename: Iu I
authors.initials: IuI
authors.lastname: Slepokurova
authors.forename: V F
authors.initials: VF
authors.lastname: Selemenev
authors.forename: I V
authors.initials: IV
authors.lastname: Shkutina
authors.forename: O F
authors.initials: OF
authors.lastname: Stoianova
mesh_terms: D001230:Aspergillus / Q000201:enzymology*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000302:isolation & purification*; D005087:Glucan 1,4-alpha-Glucosidase / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D005087:Glucan 1,4-alpha-Glucosidase