Electrochemically synthesized polyaniline as support for lipase immobilization
Authorized Users Only
2011
Authors
Bezbradica, Dejan
Jugović, Branimir

Gvozdenović, Milica M.

Jakovetić, Sonja

Knežević Jugović, Zorica

Article (Published version)

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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.
Keywords:
lipase / amination / polyaniline / electrochemical synthesis / galvanostatic techniqueSource:
Journal of Molecular Catalysis B: Enzymatic, 2011, 55-60Publisher:
- Elsevier
Funding / projects:
DOI: 10.1016/j.molcatb.2011.02.004
ISSN: 1381-1177
WoS: 000289453100008
Scopus: 2-s2.0-79952816284
Institution/Community
Институт техничких наука САНУ / Institute of Technical Sciences of SASATY - JOUR AU - Bezbradica, Dejan AU - Jugović, Branimir AU - Gvozdenović, Milica M. AU - Jakovetić, Sonja AU - Knežević Jugović, Zorica PY - 2011 UR - https://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 UR - https://hdl.handle.net/21.15107/rcub_dais_702 ER -
@article{ author = "Bezbradica, Dejan and Jugović, Branimir and Gvozdenović, Milica M. and Jakovetić, Sonja and Knežević Jugović, Zorica", year = "2011", 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", url = "https://hdl.handle.net/21.15107/rcub_dais_702" }
Bezbradica, D., Jugović, B., Gvozdenović, M. M., Jakovetić, S.,& Knežević Jugović, Z.. (2011). Electrochemically synthesized polyaniline as support for lipase immobilization. in Journal of Molecular Catalysis B: Enzymatic Elsevier., 55-60. https://doi.org/10.1016/j.molcatb.2011.02.004 https://hdl.handle.net/21.15107/rcub_dais_702
Bezbradica D, Jugović B, Gvozdenović MM, Jakovetić S, Knežević Jugović Z. Electrochemically synthesized polyaniline as support for lipase immobilization. in Journal of Molecular Catalysis B: Enzymatic. 2011;:55-60. doi:10.1016/j.molcatb.2011.02.004 https://hdl.handle.net/21.15107/rcub_dais_702 .
Bezbradica, Dejan, Jugović, Branimir, Gvozdenović, Milica M., Jakovetić, Sonja, Knežević Jugović, Zorica, "Electrochemically synthesized polyaniline as support for lipase immobilization" in Journal of Molecular Catalysis B: Enzymatic (2011):55-60, https://doi.org/10.1016/j.molcatb.2011.02.004 ., https://hdl.handle.net/21.15107/rcub_dais_702 .