Electrochemically synthesized polyaniline as support for lipase immobilization
Само за регистроване кориснике
2011
Аутори
Bezbradica, DejanJugović, Branimir
Gvozdenović, Milica
Jakovetić, Sonja
Knežević-Jugović, Zorica
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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 am...ination, especially if immobilization was performed at pH 10, so in such a way obtained derivative retained 91% of activity after 15 reaction cycles.
Кључне речи:
Lipase / Amination / Polyaniline / Electrochemical synthesis / Galvanostatic techniqueИзвор:
Journal of Molecular Catalysis B-Enzymatic, 2011, 70, 1-2, 55-60Издавач:
- Elsevier Science Bv, Amsterdam
Финансирање / пројекти:
DOI: 10.1016/j.molcatb.2011.02.004
ISSN: 1381-1177
WoS: 000289453100008
Scopus: 2-s2.0-79952816284
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Bezbradica, Dejan AU - Jugović, Branimir AU - Gvozdenović, Milica AU - Jakovetić, Sonja AU - Knežević-Jugović, Zorica PY - 2011 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1952 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 Science Bv, Amsterdam T2 - Journal of Molecular Catalysis B-Enzymatic T1 - Electrochemically synthesized polyaniline as support for lipase immobilization EP - 60 IS - 1-2 SP - 55 VL - 70 DO - 10.1016/j.molcatb.2011.02.004 ER -
@article{ author = "Bezbradica, Dejan and Jugović, Branimir and Gvozdenović, Milica 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 Science Bv, Amsterdam", journal = "Journal of Molecular Catalysis B-Enzymatic", title = "Electrochemically synthesized polyaniline as support for lipase immobilization", pages = "60-55", number = "1-2", volume = "70", doi = "10.1016/j.molcatb.2011.02.004" }
Bezbradica, D., Jugović, B., Gvozdenović, M., Jakovetić, S.,& Knežević-Jugović, Z.. (2011). Electrochemically synthesized polyaniline as support for lipase immobilization. in Journal of Molecular Catalysis B-Enzymatic Elsevier Science Bv, Amsterdam., 70(1-2), 55-60. https://doi.org/10.1016/j.molcatb.2011.02.004
Bezbradica D, Jugović B, Gvozdenović M, Jakovetić S, Knežević-Jugović Z. Electrochemically synthesized polyaniline as support for lipase immobilization. in Journal of Molecular Catalysis B-Enzymatic. 2011;70(1-2):55-60. doi:10.1016/j.molcatb.2011.02.004 .
Bezbradica, Dejan, Jugović, Branimir, Gvozdenović, Milica, Jakovetić, Sonja, Knežević-Jugović, Zorica, "Electrochemically synthesized polyaniline as support for lipase immobilization" in Journal of Molecular Catalysis B-Enzymatic, 70, no. 1-2 (2011):55-60, https://doi.org/10.1016/j.molcatb.2011.02.004 . .