Bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powder
The aim of the present study was to evaluate the efficacy of peroxidase immobilized on corncob powder for the discoloration of dye. Peroxidase was extracted from soybean seed coat, followed by amination of the surface of the tertiary structure. The aminated peroxidase was immobilized on highly activ...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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São Paulo State University (UNESP)
2013-07-01
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| Series: | Revista de Ciências Farmacêuticas Básica e Aplicada |
| Subjects: | |
| Online Access: | http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/191 |
| _version_ | 1818339169730035712 |
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| author | Júlio César Vinueza Galárraga Andréa Francisco dos Santos Juliana Cristina Bassan Antonio José Goulart Rubens Monti |
| author_facet | Júlio César Vinueza Galárraga Andréa Francisco dos Santos Juliana Cristina Bassan Antonio José Goulart Rubens Monti |
| author_sort | Júlio César Vinueza Galárraga |
| collection | DOAJ |
| description | The aim of the present study was to evaluate the efficacy of peroxidase immobilized on corncob powder for the discoloration of dye. Peroxidase was extracted from soybean seed coat, followed by amination of the surface of the tertiary structure. The aminated peroxidase was immobilized on highly activated corncob powder and employed for the discoloration of bromophenol blue. Amination was performed with 10 or 50 mmol.L-1 carbodiimide and 1 mol.L-1ethylenediamine. The amount of protein in the extract was 0.235 ± 0.011 mg.mL-1 and specific peroxidase activity was 86.06 ± 1.52 µmol min-1. mg-1, using 1 mmol.L-1 ABTS as substrate. Ten mmol.L-1 and 50 mmol.L-1 aminated peroxidase retained 88 and 100% of the initial activity. Following covalent immobilization on a corncob powder-glyoxyl support, 10 and 50 mmol.L-1 aminated peroxidase retained 74 and 86% of activity, respectively. Derivatives were used for the discoloration of 0.02 mmol.L-1 bromophenol blue solution. After 30 min, 93 and 89% discoloration was achieved with the 10 mmol.L-1 and 50 mmol.L-1 derivatives, respectively. Moreover, these derivatives retained 60% of the catalytic properties when used three times. Peroxidase extracted from soybean seed coat immobilized on a low-cost corncob powder support exhibited improved thermal stability. |
| first_indexed | 2024-12-13T15:22:44Z |
| format | Article |
| id | doaj.art-b174fa9de3794388a9b8adc134dc80a0 |
| institution | Directory Open Access Journal |
| issn | 1808-4532 2179-443X |
| language | English |
| last_indexed | 2024-12-13T15:22:44Z |
| publishDate | 2013-07-01 |
| publisher | São Paulo State University (UNESP) |
| record_format | Article |
| series | Revista de Ciências Farmacêuticas Básica e Aplicada |
| spelling | doaj.art-b174fa9de3794388a9b8adc134dc80a02022-12-21T23:40:30ZengSão Paulo State University (UNESP)Revista de Ciências Farmacêuticas Básica e Aplicada1808-45322179-443X2013-07-01343191Bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powderJúlio César Vinueza GalárragaAndréa Francisco dos SantosJuliana Cristina BassanAntonio José GoulartRubens MontiThe aim of the present study was to evaluate the efficacy of peroxidase immobilized on corncob powder for the discoloration of dye. Peroxidase was extracted from soybean seed coat, followed by amination of the surface of the tertiary structure. The aminated peroxidase was immobilized on highly activated corncob powder and employed for the discoloration of bromophenol blue. Amination was performed with 10 or 50 mmol.L-1 carbodiimide and 1 mol.L-1ethylenediamine. The amount of protein in the extract was 0.235 ± 0.011 mg.mL-1 and specific peroxidase activity was 86.06 ± 1.52 µmol min-1. mg-1, using 1 mmol.L-1 ABTS as substrate. Ten mmol.L-1 and 50 mmol.L-1 aminated peroxidase retained 88 and 100% of the initial activity. Following covalent immobilization on a corncob powder-glyoxyl support, 10 and 50 mmol.L-1 aminated peroxidase retained 74 and 86% of activity, respectively. Derivatives were used for the discoloration of 0.02 mmol.L-1 bromophenol blue solution. After 30 min, 93 and 89% discoloration was achieved with the 10 mmol.L-1 and 50 mmol.L-1 derivatives, respectively. Moreover, these derivatives retained 60% of the catalytic properties when used three times. Peroxidase extracted from soybean seed coat immobilized on a low-cost corncob powder support exhibited improved thermal stability.http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/191peroxidases. multipoint immobilization of enzymes. aminated enzymes. corncob powder. |
| spellingShingle | Júlio César Vinueza Galárraga Andréa Francisco dos Santos Juliana Cristina Bassan Antonio José Goulart Rubens Monti Bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powder Revista de Ciências Farmacêuticas Básica e Aplicada peroxidases. multipoint immobilization of enzymes. aminated enzymes. corncob powder. |
| title | Bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powder |
| title_full | Bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powder |
| title_fullStr | Bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powder |
| title_full_unstemmed | Bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powder |
| title_short | Bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powder |
| title_sort | bromophenol blue discoloration using peroxidase immobilized on highly activated corncob powder |
| topic | peroxidases. multipoint immobilization of enzymes. aminated enzymes. corncob powder. |
| url | http://rcfba.fcfar.unesp.br/index.php/ojs/article/view/191 |
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