Enzyme-Catalyzed Oxidation of 17β-Estradiol Using Immobilized Laccase from Trametes versicolor
| Autor: | Jim A. Nicell, Chantale Cardinal-Watkins |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
0106 biological sciences
Article Subject 010501 environmental sciences 01 natural sciences Biochemistry Catalysis Reaction rate lcsh:Biochemistry 010608 biotechnology Oxidative enzyme lcsh:QD415-436 Molecular Biology lcsh:QH301-705.5 0105 earth and related environmental sciences Trametes versicolor Packed bed Laccase Aqueous solution biology business.industry Chemistry biology.organism_classification Biotechnology lcsh:Biology (General) Covalent bond business Nuclear chemistry Research Article |
| Zdroj: | Enzyme Research Enzyme Research, Vol 2011 (2011) |
| ISSN: | 2090-0414 2090-0406 |
| Popis: | Many natural and synthetic estrogens are amenable to oxidation through the catalytic action of oxidative enzymes such as the fungal laccaseTrametes versicolor. This study focused on characterizing the conversion of estradiol (E2) using laccase that had been immobilized by covalent bonding onto silica beads contained in a bench-scale continuous-flow packed bed reactor. Conversion of E2accomplished in the reactor declined when the temperature of the system was changed from room temperature to just above freezing at pH 5 as a result of a reduced rate of reaction rather than inactivation of the enzyme. Similarly, conversion increased when the system was brought to warmer temperatures. E2conversion increased when the pH of the influent to the immobilized laccase reactor was changed from pH 7 to pH 5, but longer-term experiments showed that the enzyme is more stable at pH 7. Results also showed that the immobilized laccase maintained its activity when treating a constant supply of aqueous E2at a low mean residence time over a 12-hour period and when treating a constant supply of aqueous E2at a high mean residence time over a period of 9 days. |
| Databáze: | OpenAIRE |
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