Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions
The noncompetitive inhibition of laccase by mercury ions is reported, in particular focusing their effect over the enzyme catalytic activity. The enzymatic kinetics were obtained for different substrates (caffeic acid, gallic acid, and catechol), where caffeic acid displayed the greatest enzymatic a...
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| Format: | Article |
| Language: | English |
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Wiley
2018-01-01
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| Series: | Journal of Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2018/7462697 |
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| author | J. Juárez-Gómez E. S. Rosas-Tate G. Roa-Morales P. Balderas-Hernández M. Romero-Romo M. T. Ramírez-Silva |
| author_facet | J. Juárez-Gómez E. S. Rosas-Tate G. Roa-Morales P. Balderas-Hernández M. Romero-Romo M. T. Ramírez-Silva |
| author_sort | J. Juárez-Gómez |
| collection | DOAJ |
| description | The noncompetitive inhibition of laccase by mercury ions is reported, in particular focusing their effect over the enzyme catalytic activity. The enzymatic kinetics were obtained for different substrates (caffeic acid, gallic acid, and catechol), where caffeic acid displayed the greatest enzymatic activity. The laccase inhibition by mercury ions permitted to establish the inhibition effect through a mixed model (that actually displayed a behavior closer to that of the noncompetitive inhibitors) when evaluated by means of UV-Vis spectrophotometry, using caffeic acid as an electron donor. A mercury concentration of 2 mM led to 35% enzymatic inhibition after only a 2-minute incubation period. This method was used for quantification of mercury ions in aqueous solution, showing a detection limit of 15 ± 1 ppm. Therefore, this work presented a novel perspective for the determination of the toxic Hg(II) ions that can be readily implemented into environmental remediation methods. |
| format | Article |
| id | doaj-art-6d2ccce1174643a1b6746aa637b6560e |
| institution | OA Journals |
| issn | 2090-9063 2090-9071 |
| language | English |
| publishDate | 2018-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Chemistry |
| spelling | doaj-art-6d2ccce1174643a1b6746aa637b6560e2025-08-20T02:24:03ZengWileyJournal of Chemistry2090-90632090-90712018-01-01201810.1155/2018/74626977462697Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury IonsJ. Juárez-Gómez0E. S. Rosas-Tate1G. Roa-Morales2P. Balderas-Hernández3M. Romero-Romo4M. T. Ramírez-Silva5Departamento de Química, Universidad Autónoma Metropolitana Iztapalapa, Área de Química Analítica, San Rafael Atlixco 186, Col. Vicentina, Iztapalapa, 09340 Ciudad de México, MexicoUAEMex, Centro Conjunto de Investigación en Química Sustentable CCIQS, UAEM-UNAM, Universidad Autónoma del Estado de México, Carretera Toluca-Atlacomulco, km 14.5, 50200 Toluca, MEX, MexicoUAEMex, Centro Conjunto de Investigación en Química Sustentable CCIQS, UAEM-UNAM, Universidad Autónoma del Estado de México, Carretera Toluca-Atlacomulco, km 14.5, 50200 Toluca, MEX, MexicoUAEMex, Centro Conjunto de Investigación en Química Sustentable CCIQS, UAEM-UNAM, Universidad Autónoma del Estado de México, Carretera Toluca-Atlacomulco, km 14.5, 50200 Toluca, MEX, MexicoDepartamento de Materiales, Universidad Autónoma Metropolitana-Azcapotzalco, Av. San Pablo 180, Col. Reynosa-Tamaulipas, Azcapotzalco, 02200 Ciudad de México, MexicoDepartamento de Química, Universidad Autónoma Metropolitana Iztapalapa, Área de Química Analítica, San Rafael Atlixco 186, Col. Vicentina, Iztapalapa, 09340 Ciudad de México, MexicoThe noncompetitive inhibition of laccase by mercury ions is reported, in particular focusing their effect over the enzyme catalytic activity. The enzymatic kinetics were obtained for different substrates (caffeic acid, gallic acid, and catechol), where caffeic acid displayed the greatest enzymatic activity. The laccase inhibition by mercury ions permitted to establish the inhibition effect through a mixed model (that actually displayed a behavior closer to that of the noncompetitive inhibitors) when evaluated by means of UV-Vis spectrophotometry, using caffeic acid as an electron donor. A mercury concentration of 2 mM led to 35% enzymatic inhibition after only a 2-minute incubation period. This method was used for quantification of mercury ions in aqueous solution, showing a detection limit of 15 ± 1 ppm. Therefore, this work presented a novel perspective for the determination of the toxic Hg(II) ions that can be readily implemented into environmental remediation methods.http://dx.doi.org/10.1155/2018/7462697 |
| spellingShingle | J. Juárez-Gómez E. S. Rosas-Tate G. Roa-Morales P. Balderas-Hernández M. Romero-Romo M. T. Ramírez-Silva Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions Journal of Chemistry |
| title | Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions |
| title_full | Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions |
| title_fullStr | Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions |
| title_full_unstemmed | Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions |
| title_short | Laccase Inhibition by Mercury: Kinetics, Inhibition Mechanism, and Preliminary Application in the Spectrophotometric Quantification of Mercury Ions |
| title_sort | laccase inhibition by mercury kinetics inhibition mechanism and preliminary application in the spectrophotometric quantification of mercury ions |
| url | http://dx.doi.org/10.1155/2018/7462697 |
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