Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays

Uroš Andjelković; Aleksandra Milutinović-Nikolić; Nataša Jović-Jovičić; Predrag Banković; Teja Bajt; Zorica Mojović; Zoran Vujčić; Dušan Jovanović

doi:10.1016/j.foodchem.2014.07.055

Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays

Food Chem. 2015 Feb 1:168:262-9. doi: 10.1016/j.foodchem.2014.07.055. Epub 2014 Jul 15.

Authors

Uroš Andjelković¹, Aleksandra Milutinović-Nikolić², Nataša Jović-Jovičić², Predrag Banković³, Teja Bajt⁴, Zorica Mojović², Zoran Vujčić⁵, Dušan Jovanović²

Affiliations

¹ 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.
² Department of Catalysis and Chemical Engineering, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, 11000 Belgrade, Serbia.
³ 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.
⁴ Department of Biochemistry, Molecular and Structural Biology, Institute Jožef Stefan, Jamova 39, 1000 Ljubljana, Slovenia.
⁵ Department of Biochemistry, Faculty of Chemistry, University of Belgrade, Studentski trg 12-16, 11000 Belgrade, Serbia.

PMID: 25172709
DOI: 10.1016/j.foodchem.2014.07.055

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.

Keywords: Beidellite; Immobilisation; Invertase; Nanoclay; Sucrose hydrolysis.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Aluminum Silicates
Catalysis
Clay
Enzyme Stability
Enzymes, Immobilized / chemistry*
Hydrogen-Ion Concentration
Nanostructures
Saccharomyces cerevisiae / enzymology*
Spectroscopy, Fourier Transform Infrared
X-Ray Diffraction
beta-Fructofuranosidase / chemistry*

Substances

Aluminum Silicates
Enzymes, Immobilized
beidellite
beta-Fructofuranosidase
Clay