Preparation and characterization of stable cross-linked enzyme aggregates of novel laccase enzyme from Shewanella putrefaciens and using malachite green decolorization
| Autor: | Zeynep Aydin Sinirlioglu, Deniz Sinirlioglu, Fahri Akbas |
|---|---|
| Přispěvatelé: | AKBAŞ, FAHRİ |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Environmental Engineering
Bioengineering Shewanella putrefaciens medicine.disease_cause Catalysis chemistry.chemical_compound Escherichia coli Rosaniline Dyes medicine Organic chemistry Ammonium Cloning Molecular Malachite green Coloring Agents Waste Management and Disposal chemistry.chemical_classification Laccase biology Renewable Energy Sustainability and the Environment Temperature General Medicine Hydrogen-Ion Concentration Enzymes Immobilized biology.organism_classification Recombinant Proteins Enzyme assay Kinetics Chloramphenicol Cross-Linking Reagents Enzyme chemistry Glutaral biology.protein Electrophoresis Polyacrylamide Gel Glutaraldehyde Nuclear chemistry |
| Popis: | A novel type laccase from Shewanella putrefaciens was identified, expressed in Escherichia coli, characterized, prepared in cross-linked enzyme aggregates (CLEA) for industrial applications and investigated of decolorization activity on malchite green dye. Enzyme characterization was investigated by enzyme assay, SDS-PAGE and other biochemical reactions. Moreover, cross-linked enzyme aggregates were prepared and characterized. Saturated ammonium sulphate solution was used as the precipitating agent and cross linked with glutaraldehyde. These CLEA-laccase aggregates showed more catalytic efficiency and more stabilities compared to free laccase against harsh conditions of thermal and chemical agents as well as high reusability. Also it showed more decolorization ability. These results suggest that this CLEA is potentially usable in industrial applications. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|