IMOBILIZAÇÃO DE PEROXIDASE DE RAIZ FORTE EM BAGAÇO DE CANA-DE-AÇÚCAR
The immobilization of horseradish peroxidase (HRP) on raw and alkaline pre-treated sugarcane bagasse by physical adsorption (ADS) and covalent bond (LC) methods was studied. The saturation of the support with 2 mg of HRP/g of support by LC immobilization reached 35% of immobilization efficiency and...
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Sociedade Brasileira de Química
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Series: | Química Nova |
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Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422018000901019&lng=en&tlng=en |
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author | Monna Lisa B. Queiroz Kennedy C. da Conceição Micael Nunes Melo Osmar Calderón Sánchez Heiddy M. Alvarez Cleide M. F. Soares Alini T. Fricks |
author_facet | Monna Lisa B. Queiroz Kennedy C. da Conceição Micael Nunes Melo Osmar Calderón Sánchez Heiddy M. Alvarez Cleide M. F. Soares Alini T. Fricks |
author_sort | Monna Lisa B. Queiroz |
collection | DOAJ |
description | The immobilization of horseradish peroxidase (HRP) on raw and alkaline pre-treated sugarcane bagasse by physical adsorption (ADS) and covalent bond (LC) methods was studied. The saturation of the support with 2 mg of HRP/g of support by LC immobilization reached 35% of immobilization efficiency and 39 units of the immobilized enzyme (U). Regarding the HRP immobilization on sugarcane bagasse without pretreatment and using the same HRP loading, it was observed a reduction in the efficiency of immobilization and in the number of immobilized units for both methods, ADS (13.98% and 15.46 U) and LC (15.79% and 17.46 U). The sugarcane bagasse with alkaline pretreatment experiment, on the other hand, exhibited higher potential for HRP immobilization by LC. The supports and biocatalysts were characterized by Fourier transform infrared spectroscopy (FTIR), showing greater availability of hydroxyl groups in the pretreated support and the typical amide I and amide II bands that corroborate the effectiveness of the enzyme immobilization on sugarcane bagasse. In the same way, the thermogravimetric analysis (TGA) confirmed a higher weight loss in the region I for the derivative immobilized by LC, suggesting the presence of water favored enzymatic activity. |
first_indexed | 2024-12-12T13:59:15Z |
format | Article |
id | doaj.art-e6518ebb449c406cb6fc9156ace15d1f |
institution | Directory Open Access Journal |
issn | 1678-7064 |
language | English |
last_indexed | 2024-12-12T13:59:15Z |
publisher | Sociedade Brasileira de Química |
record_format | Article |
series | Química Nova |
spelling | doaj.art-e6518ebb449c406cb6fc9156ace15d1f2022-12-22T00:22:24ZengSociedade Brasileira de QuímicaQuímica Nova1678-70644191019102410.21577/0100-4042.20170279S0100-40422018000901019IMOBILIZAÇÃO DE PEROXIDASE DE RAIZ FORTE EM BAGAÇO DE CANA-DE-AÇÚCARMonna Lisa B. QueirozKennedy C. da ConceiçãoMicael Nunes MeloOsmar Calderón SánchezHeiddy M. AlvarezCleide M. F. SoaresAlini T. FricksThe immobilization of horseradish peroxidase (HRP) on raw and alkaline pre-treated sugarcane bagasse by physical adsorption (ADS) and covalent bond (LC) methods was studied. The saturation of the support with 2 mg of HRP/g of support by LC immobilization reached 35% of immobilization efficiency and 39 units of the immobilized enzyme (U). Regarding the HRP immobilization on sugarcane bagasse without pretreatment and using the same HRP loading, it was observed a reduction in the efficiency of immobilization and in the number of immobilized units for both methods, ADS (13.98% and 15.46 U) and LC (15.79% and 17.46 U). The sugarcane bagasse with alkaline pretreatment experiment, on the other hand, exhibited higher potential for HRP immobilization by LC. The supports and biocatalysts were characterized by Fourier transform infrared spectroscopy (FTIR), showing greater availability of hydroxyl groups in the pretreated support and the typical amide I and amide II bands that corroborate the effectiveness of the enzyme immobilization on sugarcane bagasse. In the same way, the thermogravimetric analysis (TGA) confirmed a higher weight loss in the region I for the derivative immobilized by LC, suggesting the presence of water favored enzymatic activity.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422018000901019&lng=en&tlng=ensugarcane bagasseimmobilizationhorseradish peroxidase |
spellingShingle | Monna Lisa B. Queiroz Kennedy C. da Conceição Micael Nunes Melo Osmar Calderón Sánchez Heiddy M. Alvarez Cleide M. F. Soares Alini T. Fricks IMOBILIZAÇÃO DE PEROXIDASE DE RAIZ FORTE EM BAGAÇO DE CANA-DE-AÇÚCAR Química Nova sugarcane bagasse immobilization horseradish peroxidase |
title | IMOBILIZAÇÃO DE PEROXIDASE DE RAIZ FORTE EM BAGAÇO DE CANA-DE-AÇÚCAR |
title_full | IMOBILIZAÇÃO DE PEROXIDASE DE RAIZ FORTE EM BAGAÇO DE CANA-DE-AÇÚCAR |
title_fullStr | IMOBILIZAÇÃO DE PEROXIDASE DE RAIZ FORTE EM BAGAÇO DE CANA-DE-AÇÚCAR |
title_full_unstemmed | IMOBILIZAÇÃO DE PEROXIDASE DE RAIZ FORTE EM BAGAÇO DE CANA-DE-AÇÚCAR |
title_short | IMOBILIZAÇÃO DE PEROXIDASE DE RAIZ FORTE EM BAGAÇO DE CANA-DE-AÇÚCAR |
title_sort | imobilizacao de peroxidase de raiz forte em bagaco de cana de acucar |
topic | sugarcane bagasse immobilization horseradish peroxidase |
url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422018000901019&lng=en&tlng=en |
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