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

•Yeast external invertase isoform 1 was immobilised on modified beidellite nanoclays.•Adsorption capacity of beidellite was significantly influenced by chemical modification.•The immobilisation improved thermal and storage stability of invertase.•Beidellite nanoclays can be modified to be used as ef...

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Published in:Food chemistry 2015-02, Vol.168, p.262-269
Main Authors: Andjelković, Uroš, Milutinović-Nikolić, Aleksandra, Jović-Jovičić, Nataša, Banković, Predrag, Bajt, Teja, Mojović, Zorica, Vujčić, Zoran, Jovanović, Dušan
Format: Article
Language:English
Subjects:
Aluminum Silicates
Beidellite
beta-Fructofuranosidase - chemistry
Biological and medical sciences
Catalysis
Enzyme Stability
Enzymes, Immobilized - chemistry
Food toxicology
Hydrogen-Ion Concentration
Immobilisation
Invertase
Medical sciences
Nanoclay
Nanostructures
Saccharomyces cerevisiae - enzymology
Spectroscopy, Fourier Transform Infrared
Sucrose hydrolysis
Toxicology
X-Ray Diffraction
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Summary:•Yeast external invertase isoform 1 was immobilised on modified beidellite nanoclays.•Adsorption capacity of beidellite was significantly influenced by chemical modification.•The immobilisation improved thermal and storage stability of invertase.•Beidellite nanoclays can be modified to be used as efficient enzyme supports. 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.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2014.07.055