title: Covalent Immobilization of Enzymes on Eupergit®Supports: Effect of the Immobilization Protocol.
abstract: A selection of best combination of adequate immobilization support and efficient immobilization method is still a key requirement for successful application of immobilized enzymes on an industrial level. Eupergit®supports exhibit good mechanical and chemical properties and allow establishment of satisfactory hydrodynamic regime in enzyme reactors. This is advantageous for their wide application in enzyme immobilization after finding the most favorable immobilization method. Methods for enzyme immobilization that have been previously reported as efficient considering the obtained activity of immobilized enzyme are presented: direct binding to polymers via their epoxy groups, binding to polymers via a spacer made from ethylene diamine/glutaraldehyde, and coupling the periodate-oxidized sugar moieties of the enzymes to the polymer beads. The modification of the conventionally immobilized enzyme with ethylenediamine via the carbodiimide route seems to be a powerful tool to improve its stability and catalytic activity.
authors: Department for Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, Belgrade, Serbia. zknez@tmf.bg.ac.rs.
authors: Zorica D
authors: ZD
authors: Knežević-Jugović
authors: Faculty of Technology and Metallurgy, Innovation Centre, University of Belgrade, Karnegijeva 4, Belgrade, Serbia.
authors: Sanja Ž
authors: SŽ
authors: Grbavčić
authors: Department for Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, Belgrade, Serbia.
authors: Jelena R
authors: JR
authors: Jovanović
authors: Department for Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, Belgrade, Serbia.
authors: Andrea B
authors: AB
authors: Stefanović
authors: Department for Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, Belgrade, Serbia.
authors: Dejan I
authors: DI
authors: Bezbradica
authors: Department for Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, Belgrade, Serbia.
authors: Dušan Ž
authors: DŽ
authors: Mijin
authors: Faculty of Technology, University of Novi Sad, Blvd. Cara Lazara 1, Novi Sad, Serbia.
authors: Mirjana G
authors: MG
authors: Antov
mesh_terms: D000178:Acrylamides / Q000737:chemistry; D000586:Amination; D002175:Candida / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D004852:Epoxy Compounds / Q000737:chemistry*; D005029:Ethylenediamines / Q000737:chemistry*; D005976:Glutaral / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008689:Methacrylates / Q000737:chemistry; D010084:Oxidation-Reduction; D011108:Polymers / Q000737:chemistry*
chemical_list: D000178:Acrylamides; D004800:Enzymes, Immobilized; D004852:Epoxy Compounds; D005029:Ethylenediamines; D008689:Methacrylates; D011108:Polymers; C031234:ethylenediamine; C065843:Eupergit C; D008049:Lipase; C045985:methacrylamide; D005976:Glutaral
keywords: Aminated support; Carbodiimide chemistry; Covalent immobilization; Enzyme chemical amination; Epoxy groups; Eupergit C; Glycoenzymes; Multipoint covalent attachment; Periodate oxidation