Improvement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methods
The immobilization and stabilization of Aspergillus oryzae β-galactosidase on DuoliteA568 was achieved using a combination of physical adsorption, incubation step in buffer at pH 9.0 and cross-linking with glutaraldehyde and in this sequence promoted a 44% increase in enzymatic activity as compare...
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| Language: | English |
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Association of the Chemical Engineers of Serbia
2017-01-01
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| Series: | Chemical Industry and Chemical Engineering Quarterly |
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| Online Access: | http://www.doiserbia.nb.rs/img/doi/1451-9372/2017/1451-93721700010F.pdf |
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| author | Falleiros Larissa Nayhara Soares Santana Cabral Bruna Vieira Fischer Janaína Guidini Carla Zanella Cardoso Vicelma Luiz de Resende Miriam Maria Ribeiro Eloízio Júlio |
| author_facet | Falleiros Larissa Nayhara Soares Santana Cabral Bruna Vieira Fischer Janaína Guidini Carla Zanella Cardoso Vicelma Luiz de Resende Miriam Maria Ribeiro Eloízio Júlio |
| author_sort | Falleiros Larissa Nayhara Soares Santana |
| collection | DOAJ |
| description | The immobilization and stabilization of Aspergillus oryzae β-galactosidase on DuoliteA568 was achieved using a combination of physical adsorption, incubation step in buffer at pH 9.0 and cross-linking with glutaraldehyde and in this sequence promoted a 44% increase in enzymatic activity as compared with the biocatalyst obtained after a two-step immobilization process (adsorption and cross-linking). The stability of the biocatalyst obtained by three-step immobilization process (adsorption, incubation in buffer at pH 9.0 and cross-linking) was higher than that obtained by two-steps (adsorption and cross-linking) and for free enzyme in relation to pH, storage and reusability. The immobilized biocatalyst was characterized with respect to thermal stability in the range 55-65 °C. The kinetics of thermal deactivation was well described by the first-order model, which resulted in the immobilized biocatalyst activation energy of thermal deactivation of 71.03 kcal/mol and 5.48 h half-life at 55.0 °C. |
| first_indexed | 2024-12-10T12:37:42Z |
| format | Article |
| id | doaj.art-69c2f77cdfed41179ebff176ca5c7448 |
| institution | Directory Open Access Journal |
| issn | 1451-9372 2217-7434 |
| language | English |
| last_indexed | 2024-12-10T12:37:42Z |
| publishDate | 2017-01-01 |
| publisher | Association of the Chemical Engineers of Serbia |
| record_format | Article |
| series | Chemical Industry and Chemical Engineering Quarterly |
| spelling | doaj.art-69c2f77cdfed41179ebff176ca5c74482022-12-22T01:48:36ZengAssociation of the Chemical Engineers of SerbiaChemical Industry and Chemical Engineering Quarterly1451-93722217-74342017-01-0123449550610.2298/CICEQ160912010F1451-93721700010FImprovement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methodsFalleiros Larissa Nayhara Soares Santana0Cabral Bruna Vieira1Fischer Janaína2Guidini Carla Zanella3Cardoso Vicelma Luiz4de Resende Miriam Maria5Ribeiro Eloízio Júlio6Uberlândia Federal University, Faculty of Chemical Engineering, Campus Santa Mônica-Bloco K, Uberlândia, BrazilUberlândia Federal University, Faculty of Chemical Engineering, Campus Santa Mônica-Bloco K, Uberlândia, BrazilUberlândia Federal University, Faculty of Chemical Engineering, Campus Santa Mônica-Bloco K, Uberlândia, BrazilUberlândia Federal University, Faculty of Chemical Engineering, Campus Santa Mônica-Bloco K, Uberlândia, BrazilUberlândia Federal University, Faculty of Chemical Engineering, Campus Santa Mônica-Bloco K, Uberlândia, BrazilUberlândia Federal University, Faculty of Chemical Engineering, Campus Santa Mônica-Bloco K, Uberlândia, BrazilUberlândia Federal University, Faculty of Chemical Engineering, Campus Santa Mônica-Bloco K, Uberlândia, BrazilThe immobilization and stabilization of Aspergillus oryzae β-galactosidase on DuoliteA568 was achieved using a combination of physical adsorption, incubation step in buffer at pH 9.0 and cross-linking with glutaraldehyde and in this sequence promoted a 44% increase in enzymatic activity as compared with the biocatalyst obtained after a two-step immobilization process (adsorption and cross-linking). The stability of the biocatalyst obtained by three-step immobilization process (adsorption, incubation in buffer at pH 9.0 and cross-linking) was higher than that obtained by two-steps (adsorption and cross-linking) and for free enzyme in relation to pH, storage and reusability. The immobilized biocatalyst was characterized with respect to thermal stability in the range 55-65 °C. The kinetics of thermal deactivation was well described by the first-order model, which resulted in the immobilized biocatalyst activation energy of thermal deactivation of 71.03 kcal/mol and 5.48 h half-life at 55.0 °C.http://www.doiserbia.nb.rs/img/doi/1451-9372/2017/1451-93721700010F.pdfβ-galactosidaseDuolite A-568immobilizationincubation in buffer at pH 9.0 |
| spellingShingle | Falleiros Larissa Nayhara Soares Santana Cabral Bruna Vieira Fischer Janaína Guidini Carla Zanella Cardoso Vicelma Luiz de Resende Miriam Maria Ribeiro Eloízio Júlio Improvement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methods Chemical Industry and Chemical Engineering Quarterly β-galactosidase Duolite A-568 immobilization incubation in buffer at pH 9.0 |
| title | Improvement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methods |
| title_full | Improvement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methods |
| title_fullStr | Improvement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methods |
| title_full_unstemmed | Improvement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methods |
| title_short | Improvement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methods |
| title_sort | improvement of recovered activity and stability of the aspergillus oryzae β galactosidase immobilized on duolite a568 by combination of immobilization methods |
| topic | β-galactosidase Duolite A-568 immobilization incubation in buffer at pH 9.0 |
| url | http://www.doiserbia.nb.rs/img/doi/1451-9372/2017/1451-93721700010F.pdf |
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