Electrochemically synthesized polyaniline as support for lipase immobilization
Samo za registrovane korisnike
2011
Autori
Bezbradica, DejanJugović, Branimir

Gvozdenović, Milica M.
Jakovetić, Sonja

Knežević Jugović, Zorica

Članak u časopisu (Objavljena verzija)

Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
lipase / amination / polyaniline / electrochemical synthesis / galvanostatic techniqueIzvor:
Journal of Molecular Catalysis B: Enzymatic, 2011, 55-60Izdavač:
- Elsevier
Projekti:
DOI: 10.1016/j.molcatb.2011.02.004
ISSN: 1381-1177
WoS: 000289453100008
Scopus: 2-s2.0-79952816284
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 .