Optical detection of different phenolic compounds by means of a novel biosensor based on sol-gel immobilized laccase

A novel sol-gel based biosensor exploiting the optical absorption properties of sol-gel immobilized laccase has been constructed in the attempt to increase enzyme specificity towards different phenolic substrates. Laccase from Trametes versicolor has been immobilized in optically transparent sol-gel matrices. Using Fourier transform infrared spectroscopy and data analysis based on a wavelet algorithm the successful enzyme immobilization has been evidenced. The changes in the optical absorption spectra of laccase reaction products at 425 nm, 375 nm and 400 nm have been used for hydroquinone, resorcinol and catechol concentration determination, respectively. Due to the slow response time of hydroquinone-laccase reaction, our optical biosensor has been tested with resorcinol and catechol. Linear ranges up to 1.4 mM and 0.2 mM, limit-of-detection (LOD) of 4.5 μM and 0.6 μΜ have been evidenced for resorcinol and catechol, respectively. Data for resorcinol concentration determination have been particularly interesting since no other biosensor device has been reported in literature. In comparison with other biosensors using laccase from the same native source our biosensor has been characterized by larger linear ranges, significant sensitivities and good LODs. To challenge our biosensor with real samples, tap water samples spiked with known amount of catechol and resorcinol have been employed. This article is protected by copyright. All rights reserved.