title: Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays.
abstract: The external invertase isoform 1 (EINV1) was immobilised on eight differently modified beidellite nanoclays. Modifications were composed of organo-modification with different amounts of surfactant - hexadecyl trimethylammonium cation (HDTMA), pillaring with Al/Fe containing polyhydroxy cations and acid modification of Na-enriched and pillared clays. The modified nanoclays were characterised by XRD, N2-physisorption, SEM and FT-IR spectroscopy. The amount of bound enzyme activity was significantly influenced by the modification of beidellite ranging from 50 to remarkable 2200U/g. Biochemical characterization was performed for five modified nanoclays showing the highest enzyme activity after invertase immobilisation. The investigation demonstrated that after immobilisation the structure and the catalytic properties of invertase were preserved, while Km values were slightly increased from 26 to 37mM. immobilisation significantly improved thermal and storage stability of EINV1. Results indicate that beidellite nanoclays obtained by low cost modifications can be applied as a suitable support for the immobilisation of invertase. The immobilizate can be efficiently engaged in sucrose hydrolysis in batch reactor.
authors.affiliation: Department of Chemistry, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Studentski trg 12-16, 11000 Belgrade, Serbia. Electronic address: uros@chem.bg.ac.rs.
authors.forename: Uroš
authors.initials: U
authors.lastname: Andjelković
authors.affiliation: Department of Catalysis and Chemical Engineering, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, 11000 Belgrade, Serbia.
authors.forename: Aleksandra
authors.initials: A
authors.lastname: Milutinović-Nikolić
authors.affiliation: Department of Catalysis and Chemical Engineering, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, 11000 Belgrade, Serbia.
authors.forename: Nataša
authors.initials: N
authors.lastname: Jović-Jovičić
authors.affiliation: Department of Catalysis and Chemical Engineering, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, 11000 Belgrade, Serbia. Electronic address: predragb@nanosys.ihtm.bg.ac.rs.
authors.forename: Predrag
authors.initials: P
authors.lastname: Banković
authors.affiliation: Department of Biochemistry, Molecular and Structural Biology, Institute Jožef Stefan, Jamova 39, 1000 Ljubljana, Slovenia.
authors.forename: Teja
authors.initials: T
authors.lastname: Bajt
authors.affiliation: Department of Catalysis and Chemical Engineering, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, 11000 Belgrade, Serbia.
authors.forename: Zorica
authors.initials: Z
authors.lastname: Mojović
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, University of Belgrade, Studentski trg 12-16, 11000 Belgrade, Serbia.
authors.forename: Zoran
authors.initials: Z
authors.lastname: Vujčić
authors.affiliation: Department of Catalysis and Chemical Engineering, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, 11000 Belgrade, Serbia.
authors.forename: Dušan
authors.initials: D
authors.lastname: Jovanović
mesh_terms: D000538:Aluminum Silicates; D002384:Catalysis; D000077215:Clay; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D049329:Nanostructures; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D017550:Spectroscopy, Fourier Transform Infrared; D014961:X-Ray Diffraction; D043324:beta-Fructofuranosidase / Q000737:chemistry*
chemical_list: D000538:Aluminum Silicates; D004800:Enzymes, Immobilized; C010863:beidellite; D043324:beta-Fructofuranosidase; D000077215:Clay
keywords: Beidellite; Immobilisation; Invertase; Nanoclay; Sucrose hydrolysis