Immobilization of Low-Cost Alternative Vegetable Peroxidase (<i>Raphanus sativus</i> L. peroxidase): Choice of Support/Technique and Characterization
In the present work the radish (<i>Raphanus sativus</i> L.) was used as the low-cost alternative source of peroxidase. The enzyme was immobilized in different supports: coconut fiber (CF), calcium alginate microspheres (CAMs) and silica SBA-15/albumin hybrid (HB). Physical adsorption (PA...
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MDPI AG
2020-08-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/16/3668 |
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| author | Gabrielle Souza da Silva Barbosa Maria Emanuela P. S. Oliveira Ana Beatriz S. dos Santos Osmar Calderón Sánchez Cleide Mara Faria Soares Alini Tinoco Fricks |
| author_facet | Gabrielle Souza da Silva Barbosa Maria Emanuela P. S. Oliveira Ana Beatriz S. dos Santos Osmar Calderón Sánchez Cleide Mara Faria Soares Alini Tinoco Fricks |
| author_sort | Gabrielle Souza da Silva Barbosa |
| collection | DOAJ |
| description | In the present work the radish (<i>Raphanus sativus</i> L.) was used as the low-cost alternative source of peroxidase. The enzyme was immobilized in different supports: coconut fiber (CF), calcium alginate microspheres (CAMs) and silica SBA-15/albumin hybrid (HB). Physical adsorption (PA) and covalent binding (CB) as immobilization techniques were evaluated. Immobilized biocatalysts (IBs) obtained were physicochemical and morphologically characterized by SEM, FTIR and TGA. Also, optimum pH/temperature and operational stability were determined. For all supports, the immobilization by covalent binding provided the higher immobilization efficiencies—immobilization yield (IY%) of 89.99 ± 0.38% and 77.74 ± 0.42% for HB and CF, respectively. For CAMs the activity recovery (AR) was of 11.83 ± 0.68%. All IBs showed optimum pH at 6.0. Regarding optimum temperature of the biocatalysts, HB-CB and CAM-CB maintained the original optimum temperature of the free enzyme (40 °C). HB-CB showed higher operational stability, maintaining around 65% of the initial activity after four consecutive cycles. SEM, FTIR and TGA results suggest the enzyme presence on the IBs. Radish peroxidase immobilized on HB support by covalent binding is promising in future biotechnological applications. |
| first_indexed | 2024-03-10T17:35:43Z |
| format | Article |
| id | doaj.art-9b8643b51e1c4f9883a25c3c0687640b |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T17:35:43Z |
| publishDate | 2020-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-9b8643b51e1c4f9883a25c3c0687640b2023-11-20T09:53:07ZengMDPI AGMolecules1420-30492020-08-012516366810.3390/molecules25163668Immobilization of Low-Cost Alternative Vegetable Peroxidase (<i>Raphanus sativus</i> L. peroxidase): Choice of Support/Technique and CharacterizationGabrielle Souza da Silva Barbosa0Maria Emanuela P. S. Oliveira1Ana Beatriz S. dos Santos2Osmar Calderón Sánchez3Cleide Mara Faria Soares4Alini Tinoco Fricks5Programa de Pós-Graduação em Biotecnologia Industrial, Tiradentes University, 49032-490 Aracaju, SE, BrazilPrograma de Pós-Graduação em Biotecnologia Industrial, Tiradentes University, 49032-490 Aracaju, SE, BrazilPrograma de Pós-Graduação em Biotecnologia Industrial, Tiradentes University, 49032-490 Aracaju, SE, BrazilLaboratory of Organic Synthesis, Faculty of Chemistry, La Habana University, 10400 La Habana, CubaPrograma de Pós-Graduação em Biotecnologia Industrial, Tiradentes University, 49032-490 Aracaju, SE, BrazilPrograma de Pós-Graduação em Biotecnologia Industrial, Tiradentes University, 49032-490 Aracaju, SE, BrazilIn the present work the radish (<i>Raphanus sativus</i> L.) was used as the low-cost alternative source of peroxidase. The enzyme was immobilized in different supports: coconut fiber (CF), calcium alginate microspheres (CAMs) and silica SBA-15/albumin hybrid (HB). Physical adsorption (PA) and covalent binding (CB) as immobilization techniques were evaluated. Immobilized biocatalysts (IBs) obtained were physicochemical and morphologically characterized by SEM, FTIR and TGA. Also, optimum pH/temperature and operational stability were determined. For all supports, the immobilization by covalent binding provided the higher immobilization efficiencies—immobilization yield (IY%) of 89.99 ± 0.38% and 77.74 ± 0.42% for HB and CF, respectively. For CAMs the activity recovery (AR) was of 11.83 ± 0.68%. All IBs showed optimum pH at 6.0. Regarding optimum temperature of the biocatalysts, HB-CB and CAM-CB maintained the original optimum temperature of the free enzyme (40 °C). HB-CB showed higher operational stability, maintaining around 65% of the initial activity after four consecutive cycles. SEM, FTIR and TGA results suggest the enzyme presence on the IBs. Radish peroxidase immobilized on HB support by covalent binding is promising in future biotechnological applications.https://www.mdpi.com/1420-3049/25/16/3668radish peroxidaseimmobilizationsupportscharacterization |
| spellingShingle | Gabrielle Souza da Silva Barbosa Maria Emanuela P. S. Oliveira Ana Beatriz S. dos Santos Osmar Calderón Sánchez Cleide Mara Faria Soares Alini Tinoco Fricks Immobilization of Low-Cost Alternative Vegetable Peroxidase (<i>Raphanus sativus</i> L. peroxidase): Choice of Support/Technique and Characterization Molecules radish peroxidase immobilization supports characterization |
| title | Immobilization of Low-Cost Alternative Vegetable Peroxidase (<i>Raphanus sativus</i> L. peroxidase): Choice of Support/Technique and Characterization |
| title_full | Immobilization of Low-Cost Alternative Vegetable Peroxidase (<i>Raphanus sativus</i> L. peroxidase): Choice of Support/Technique and Characterization |
| title_fullStr | Immobilization of Low-Cost Alternative Vegetable Peroxidase (<i>Raphanus sativus</i> L. peroxidase): Choice of Support/Technique and Characterization |
| title_full_unstemmed | Immobilization of Low-Cost Alternative Vegetable Peroxidase (<i>Raphanus sativus</i> L. peroxidase): Choice of Support/Technique and Characterization |
| title_short | Immobilization of Low-Cost Alternative Vegetable Peroxidase (<i>Raphanus sativus</i> L. peroxidase): Choice of Support/Technique and Characterization |
| title_sort | immobilization of low cost alternative vegetable peroxidase i raphanus sativus i l peroxidase choice of support technique and characterization |
| topic | radish peroxidase immobilization supports characterization |
| url | https://www.mdpi.com/1420-3049/25/16/3668 |
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