Electrochemical synthesis of polyaniline support for enzyme immobilization provides easier control over the properties of obtained polymer and reduced risk of biocatalyst inactivation with residues of toxic compounds. In the present study, immobilization of lipase from Candida rugosa on electrochemically synthesized PANI (activated with glutaraldehyde) resulted with high lipase loadings up to 93.7 mg of proteins per gram of dry support. The activation of support and immobilization were optimized, with respect to activity yield. The optimum concentration of glutaraldehyde was 2% (w/v) and optimum concentration of enzyme was 4 mg ml−1. Modification of enzyme surface with carbodiimide and ethylenediamine was performed in order to increase concentration of amino groups. Aminated lipase exhibited higher specific activity (52%) and thermal stability (3 times) after immobilization, compared with non-modified lipase. Also, reusability of immobilized enzyme was significantly increased with amin...ation, especially if immobilization was performed at pH 10, so in such a way obtained derivative retained 91% of activity after 15 reaction cycles.
TY - JOUR
AU - Bezbradica, Dejan
AU - Jugović, Branimir
AU - Gvozdenović, Milica M.
AU - Jakovetić, Sonja
AU - Knežević Jugović, Zorica
PY - 2011
UR - http://dais.sanu.ac.rs/123456789/702
AB - Electrochemical synthesis of polyaniline support for enzyme immobilization provides easier control over the properties of obtained polymer and reduced risk of biocatalyst inactivation with residues of toxic compounds. In the present study, immobilization of lipase from Candida rugosa on electrochemically synthesized PANI (activated with glutaraldehyde) resulted with high lipase loadings up to 93.7 mg of proteins per gram of dry support. The activation of support and immobilization were optimized, with respect to activity yield. The optimum concentration of glutaraldehyde was 2% (w/v) and optimum concentration of enzyme was 4 mg ml−1. Modification of enzyme surface with carbodiimide and ethylenediamine was performed in order to increase concentration of amino groups. Aminated lipase exhibited higher specific activity (52%) and thermal stability (3 times) after immobilization, compared with non-modified lipase. Also, reusability of immobilized enzyme was significantly increased with amination, especially if immobilization was performed at pH 10, so in such a way obtained derivative retained 91% of activity after 15 reaction cycles.
PB - Elsevier
T2 - Journal of Molecular Catalysis B: Enzymatic
T1 - Electrochemically synthesized polyaniline as support for lipase immobilization
SP - 55
EP - 60
DO - 10.1016/j.molcatb.2011.02.004
ER -
@article{
author = "Bezbradica, Dejan and Jugović, Branimir and Gvozdenović, Milica M. and Jakovetić, Sonja and Knežević Jugović, Zorica",
year = "2011",
url = "http://dais.sanu.ac.rs/123456789/702",
abstract = "Electrochemical synthesis of polyaniline support for enzyme immobilization provides easier control over the properties of obtained polymer and reduced risk of biocatalyst inactivation with residues of toxic compounds. In the present study, immobilization of lipase from Candida rugosa on electrochemically synthesized PANI (activated with glutaraldehyde) resulted with high lipase loadings up to 93.7 mg of proteins per gram of dry support. The activation of support and immobilization were optimized, with respect to activity yield. The optimum concentration of glutaraldehyde was 2% (w/v) and optimum concentration of enzyme was 4 mg ml−1. Modification of enzyme surface with carbodiimide and ethylenediamine was performed in order to increase concentration of amino groups. Aminated lipase exhibited higher specific activity (52%) and thermal stability (3 times) after immobilization, compared with non-modified lipase. Also, reusability of immobilized enzyme was significantly increased with amination, especially if immobilization was performed at pH 10, so in such a way obtained derivative retained 91% of activity after 15 reaction cycles.",
publisher = "Elsevier",
journal = "Journal of Molecular Catalysis B: Enzymatic",
title = "Electrochemically synthesized polyaniline as support for lipase immobilization",
pages = "55-60",
doi = "10.1016/j.molcatb.2011.02.004"
}
Bezbradica D, Jugović B, Gvozdenović MM, Jakovetić S, Knežević Jugović Z. Electrochemically synthesized polyaniline as support for lipase immobilization. Journal of Molecular Catalysis B: Enzymatic. 2011;:55-60
Bezbradica, D., Jugović, B., Gvozdenović, M. M., Jakovetić, S.,& Knežević Jugović, Z. (2011). Electrochemically synthesized polyaniline as support for lipase immobilization.
Journal of Molecular Catalysis B: EnzymaticElsevier., null, 55-60.
https://doi.org/10.1016/j.molcatb.2011.02.004
Bezbradica Dejan, Jugović Branimir, Gvozdenović Milica M., Jakovetić Sonja, Knežević Jugović Zorica, "Electrochemically synthesized polyaniline as support for lipase immobilization" null (2011):55-60,
https://doi.org/10.1016/j.molcatb.2011.02.004 .
