Electrochemically synthesized polyaniline as support for lipase immobilization
Autor: | Sonja M. Jakovetić, Dejan Bezbradica, Milica M. Gvozdenović, Branimir Jugović, Zorica Knežević-Jugović |
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Jazyk: | angličtina |
Rok vydání: | 2011 |
Předmět: |
Immobilized enzyme
Triacylglycerol lipase Bioengineering Ethylenediamine 02 engineering and technology 01 natural sciences Biochemistry Catalysis polyaniline galvanostatic technique electrochemical synthesis chemistry.chemical_compound Polyaniline lipase Organic chemistry Lipase Amination Carbodiimide biology Chemistry Process Chemistry and Technology 010401 analytical chemistry amination 021001 nanoscience & nanotechnology 0104 chemical sciences biology.protein Glutaraldehyde 0210 nano-technology |
Zdroj: | Journal of Molecular Catalysis B: Enzymatic Journal of Molecular Catalysis B-Enzymatic |
Popis: | 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. |
Databáze: | OpenAIRE |
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