Tannic acid interferes with the commonly used laccase-detection assay based on ABTS as the substrate
2004
Terrón, M. C. | López-Fernández, Matilde | Carbajo, J. M. | Junca, H. | Téllez, Alejandro | Yagüe, S. | Arana-Cuenca, A. | González, Tania | González, Aldo E. | Comisión Interministerial de Ciencia y Tecnología, CICYT (España) | Comunidad de Madrid | Terrón, M. C. [0000-0001-9072-8158] | López-Fernández, Matilde [0000-0002-6265-9834] | Carbajo, J. M. [0000-0002-1551-9564] | Junca, H. [0000-0003-4546-6229] | Téllez, Alejandro [0000-0002-5491-3679] | Arana-Cuenca, A. [0000-0002-3583-0237] | Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
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Show more [+] Less [-]Laccase enzymatic activity in biological samples is usually detected spectrophotometrically through its capacity to oxidize several specific aromatic compounds. One of the most commonly used substrates is the compound 2-2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), which becomes green-blue coloured when it is oxidized by laccase. In this work we study the interference of tannic acid with the spectrophotometric assay to detect laccase by using ABTS as the substrate. Our data show that under the normal reaction conditions of this assay, but in the absence of any catalyst, tannic acid is able to carry out the chemical reduction of the oxidized specie of ABTS, thus decreasing the overall detectable laccase-activity values observed when this enzyme is present in the reaction mixture. Therefore, our results represent an important warning concerning a commonly used method for measuring, detecting or screening laccases in biological samples that may content tannic acid or structural-related molecules.
Show more [+] Less [-]This work was supported by the CICYT (Madrid, Spain) BIO 97-0655 and Comunidad de Madrid (CAM 07M/0730/1997). J.M. Carbajo and M.C. Terrón acknowledge support from pre- and postdoctoral grants, from Conserjería de Educación y Cultura de la Comunidad Autónoma de Madrid (Spain).
Show more [+] Less [-]Peer reviewed
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