title: [A study of the catalytic properties of the nitrile hydratase immobilized on aluminum oxides and carbon-containing adsorbents].
abstract: The nitrile hydratase isolated from Rhodococcus ruber strain gt1, displaying a high nitrile hydratase activity, was immobilized on unmodified aluminum oxides and carbon-containing adsorbents, including the carbon carrier Sibunit. The activity and operational stability of the immobilized nitrile hydratase were studied in the reaction of acrylonitrile transformation into acrylamide. It was demonstrated that an increase in the carbon content in the carrier led to an increase in the amount of adsorbed enzyme and, concurrently, to a decrease in its activity. The nitrile hydratase immobilized on Sibunit and carbon-containing aluminum alpha-oxide having a "crust" structure displayed the highest operational stability in acrylonitrile hydration. It was shown that the thermostability of adsorbed nitrile hydratase increased by one order of magnitude.
authors.forename: Iu G
authors.initials: IuG
authors.lastname: Maksimova
authors.forename: V A
authors.initials: VA
authors.lastname: Demakov
authors.forename: A Iu
authors.initials: AIu
authors.lastname: Maksimov
authors.forename: G V
authors.initials: GV
authors.lastname: Ovechkina
authors.forename: G A
authors.initials: GA
authors.lastname: Kovalenko
mesh_terms: D000181:Acrylonitrile / Q000737:chemistry; D000327:Adsorption; D000537:Aluminum Oxide / Q000737:chemistry; D055162:Biocatalysis; D002244:Carbon / Q000737:chemistry; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006836:Hydro-Lyases / Q000737:chemistry*; D012240:Rhodococcus / Q000201:enzymology*
chemical_list: D004800:Enzymes, Immobilized; D002244:Carbon; D006836:Hydro-Lyases; C048831:nitrile hydratase; D000537:Aluminum Oxide; D000181:Acrylonitrile