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Enzymatic Reactions in Near Critical CO(2): The Effect of Pressure on Phenol Removal by Tyrosinase

The use of enzymes in supercritical CO(2) (SCCO(2)) has received extensive attention in recent years. Biocatalysts have the advantage of substrate specificity and SCCO(2) offers several advantages over liquid solvents. This work deals with the utilization of SCCO(2) as a medium for the enzymatic rem...

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Detalles Bibliográficos
Autores principales: Amaral, Priscilla, Garcia, Daniela, Cardoso, Miguel, Mendes, Marisa, Coelho, Maria Alice, Pessoa, Fernando
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2801991/
https://www.ncbi.nlm.nih.gov/pubmed/20054468
http://dx.doi.org/10.3390/ijms10125217
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author Amaral, Priscilla
Garcia, Daniela
Cardoso, Miguel
Mendes, Marisa
Coelho, Maria Alice
Pessoa, Fernando
author_facet Amaral, Priscilla
Garcia, Daniela
Cardoso, Miguel
Mendes, Marisa
Coelho, Maria Alice
Pessoa, Fernando
author_sort Amaral, Priscilla
collection PubMed
description The use of enzymes in supercritical CO(2) (SCCO(2)) has received extensive attention in recent years. Biocatalysts have the advantage of substrate specificity and SCCO(2) offers several advantages over liquid solvents. This work deals with the utilization of SCCO(2) as a medium for the enzymatic removal of phenol from aqueous solutions using tyrosinase. Since the presence of oxygen is crucial for the enzyme-catalyzed oxidation, the substantial solvating power of SCCO(2) makes it a promising medium for such reactions. The conversion of phenol was higher at 10 MPa. Under near critical conditions (7 MPa, 35 °C), the addition of air at 5 × 10(5) Pa of pressure improved phenol removal.
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spelling pubmed-28019912010-01-06 Enzymatic Reactions in Near Critical CO(2): The Effect of Pressure on Phenol Removal by Tyrosinase Amaral, Priscilla Garcia, Daniela Cardoso, Miguel Mendes, Marisa Coelho, Maria Alice Pessoa, Fernando Int J Mol Sci Article The use of enzymes in supercritical CO(2) (SCCO(2)) has received extensive attention in recent years. Biocatalysts have the advantage of substrate specificity and SCCO(2) offers several advantages over liquid solvents. This work deals with the utilization of SCCO(2) as a medium for the enzymatic removal of phenol from aqueous solutions using tyrosinase. Since the presence of oxygen is crucial for the enzyme-catalyzed oxidation, the substantial solvating power of SCCO(2) makes it a promising medium for such reactions. The conversion of phenol was higher at 10 MPa. Under near critical conditions (7 MPa, 35 °C), the addition of air at 5 × 10(5) Pa of pressure improved phenol removal. Molecular Diversity Preservation International (MDPI) 2009-12-01 /pmc/articles/PMC2801991/ /pubmed/20054468 http://dx.doi.org/10.3390/ijms10125217 Text en © 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Amaral, Priscilla
Garcia, Daniela
Cardoso, Miguel
Mendes, Marisa
Coelho, Maria Alice
Pessoa, Fernando
Enzymatic Reactions in Near Critical CO(2): The Effect of Pressure on Phenol Removal by Tyrosinase
title Enzymatic Reactions in Near Critical CO(2): The Effect of Pressure on Phenol Removal by Tyrosinase
title_full Enzymatic Reactions in Near Critical CO(2): The Effect of Pressure on Phenol Removal by Tyrosinase
title_fullStr Enzymatic Reactions in Near Critical CO(2): The Effect of Pressure on Phenol Removal by Tyrosinase
title_full_unstemmed Enzymatic Reactions in Near Critical CO(2): The Effect of Pressure on Phenol Removal by Tyrosinase
title_short Enzymatic Reactions in Near Critical CO(2): The Effect of Pressure on Phenol Removal by Tyrosinase
title_sort enzymatic reactions in near critical co(2): the effect of pressure on phenol removal by tyrosinase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2801991/
https://www.ncbi.nlm.nih.gov/pubmed/20054468
http://dx.doi.org/10.3390/ijms10125217
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