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, N-2-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 2200 U/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 37 mM. 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.
TY - JOUR
AU - Anđelković, Uroš
AU - Milutinović Nikolić, Aleksandra
AU - Jović-Jovičić, Nataša
AU - Banković, Predrag
AU - Bajt, Teja
AU - Mojović, Zorica
AU - Vujčić, Zoran
AU - Jovanović, Dušan M.
PY - 2015
UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1728
AB - 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, N-2-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 2200 U/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 37 mM. 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.
PB - Elsevier Sci Ltd, Oxford
T2 - Food Chemistry
T1 - Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays
VL - 168
SP - 262
EP - 269
DO - 10.1016/j.foodchem.2014.07.055
UR - Conv_3234
ER -
@article{
author = "Anđelković, Uroš and Milutinović Nikolić, Aleksandra and Jović-Jovičić, Nataša and Banković, Predrag and Bajt, Teja and Mojović, Zorica and Vujčić, Zoran and Jovanović, Dušan M.",
year = "2015",
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, N-2-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 2200 U/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 37 mM. 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.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays",
volume = "168",
pages = "262-269",
doi = "10.1016/j.foodchem.2014.07.055",
url = "Conv_3234"
}
Anđelković, U., Milutinović Nikolić, A., Jović-Jovičić, N., Banković, P., Bajt, T., Mojović, Z., Vujčić, Z.,& Jovanović, D. M.. (2015). Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays. in Food Chemistry
Elsevier Sci Ltd, Oxford., 168, 262-269.
https://doi.org/10.1016/j.foodchem.2014.07.055
Conv_3234
Anđelković U, Milutinović Nikolić A, Jović-Jovičić N, Banković P, Bajt T, Mojović Z, Vujčić Z, Jovanović DM. Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays. in Food Chemistry. 2015;168:262-269.
doi:10.1016/j.foodchem.2014.07.055
Conv_3234 .
Anđelković, Uroš, Milutinović Nikolić, Aleksandra, Jović-Jovičić, Nataša, Banković, Predrag, Bajt, Teja, Mojović, Zorica, Vujčić, Zoran, Jovanović, Dušan M., "Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays" in Food Chemistry, 168 (2015):262-269,
https://doi.org/10.1016/j.foodchem.2014.07.055 .,
Conv_3234 .
