Enzymatic rotating biosensor for ciprofloxacin determination

Angel Alberto Jesus Torriero, Juan J J Ruiz-Diaz, Eloy Salinas, Eduardo Marchevsky, Maria Isabel Sanz-Ferramola, Julio Raba

Research output: Contribution to journalArticleResearchpeer-review

38 Citations (Scopus)


The high sensitivity that can be attained using an enzymic system and mediated by catechol was verified by online interfacing of a rotating biosensor and continuous flow/stopped-flow/continuous-flow processing. Horseradish peroxidase, HRP [EC], immobilized on a rotating disk, in the presence of hydrogen peroxide, catalyzed the oxidn. of catechol, whose back electrochem. redn. was detected on a glassy carbon electrode surface at -200 mV. Thus, when ciprofloxacin (CF) was added to the soln., this piperazine-contg. compd. participate in Michael addn. reactions with catechol to form the corresponding piperazine-quinone derivs., decreasing the peak current obtained, in proportion with the increase of its concn. The highest response for CF was obtained around pH 7. This method could be used to det. CF concn. in the range of 0.02-65 micro M (r = 0.999). The detn. of CF concn. was possible with a detection limit of 0.4 nM, in the processing of as many as 25 samples per h. Application of this anal. to different pharmaceutical samples contg. CF supports the utility of the HRP-rotating biosensor. [on SciFinder (R)]
Original languageEnglish
Pages (from-to)691 - 699
Number of pages9
Issue number3
Publication statusPublished - 2006
Externally publishedYes

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