title: Inulinase immobilization on macroporous anion-exchange resins by different methods.
abstract: Inulinase was immobilized on AV-16-GS macroporous anion-exchange resin by physical and chemical methods. Binding of the enzyme to the carrier by the studied methods led to a shift of catalysis optimal temperature towards higher values and to extension of the range of optimum pH values. Our modification of glutaraldehyde method of inulinase immobilization increased catalytic activity of the preparation in comparison with the common glutaraldehyde method.
authors.affiliation: Voronezh State University, Russia.
authors.forename: T A
authors.initials: TA
authors.lastname: Kovaleva
authors.forename: M G
authors.initials: MG
authors.lastname: Holyavka
authors.forename: S S
authors.initials: SS
authors.lastname: Bogdanova
mesh_terms: D000837:Anion Exchange Resins; D001230:Aspergillus / Q000201:enzymology; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D005976:Glutaral / Q000737:chemistry; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration
chemical_list: D000837:Anion Exchange Resins; D004800:Enzymes, Immobilized; D006026:Glycoside Hydrolases; C023086:inulinase; D005976:Glutaral