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Enzymatic Reactions in Near Critical CO2: The Effect of Pressure on Phenol Removal by Tyrosinase
School of Chemistry, Universidade Federal do Rio de Janeiro, CT, Bl. E, Cidade Universitária, 21949-900, Rio de Janeiro, RJ, Brazil
Chemical and Biological Engineering Department, Instituto Superior Técnico, Avenida Rovisco Pais, 1049-001 Lisboa, Portugal
Chemical Engineering Department, Universidade Federal Rural do Rio de Janeiro, BR 465, Km 7, 23890, Seropédica, RJ, Brazil
* Author to whom correspondence should be addressed.
Received: 14 August 2009; in revised form: 9 November 2009 / Accepted: 16 November 2009 / Published: 1 December 2009
Abstract: The use of enzymes in supercritical CO2 (SCCO2) has received extensive attention in recent years. Biocatalysts have the advantage of substrate specificity and SCCO2 offers several advantages over liquid solvents. This work deals with the utilization of SCCO2 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 SCCO2 makes it a promising medium for such reactions. The conversion of phenol was higher at 10 MPa. Under near critical conditions (7 MPa, 35 ºC), the addition of air at 5 × 105 Pa of pressure improved phenol removal.
Keywords: tyrosinase; supercritical CO2; enzymatic reaction; phenol
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Amaral, P.; Garcia, D.; Cardoso, M.; Mendes, M.; Coelho, M.A.; Pessoa, F. Enzymatic Reactions in Near Critical CO2: The Effect of Pressure on Phenol Removal by Tyrosinase. Int. J. Mol. Sci. 2009, 10, 5217-5223.
Amaral P, Garcia D, Cardoso M, Mendes M, Coelho MA, Pessoa F. Enzymatic Reactions in Near Critical CO2: The Effect of Pressure on Phenol Removal by Tyrosinase. International Journal of Molecular Sciences. 2009; 10(12):5217-5223.
Amaral, Priscilla; Garcia, Daniela; Cardoso, Miguel; Mendes, Marisa; Coelho, Maria Alice; Pessoa, Fernando. 2009. "Enzymatic Reactions in Near Critical CO2: The Effect of Pressure on Phenol Removal by Tyrosinase." Int. J. Mol. Sci. 10, no. 12: 5217-5223.