Article

Determination of phenolic acids using Trametes versicolor laccase

ENEA, Roma, Latium, Italy
Talanta (Impact Factor: 3.51). 03/2007; 71(1):312-7. DOI: 10.1016/j.talanta.2006.04.032
Source: PubMed

ABSTRACT Two biosensors based on Trametes versicolor laccase (TvL) were developed for the determination of phenolic compounds. Commercial oxygen electrode and ferrocene-modified screen-printed graphite electrodes were used for preparation of laccase biosensors. The systems were calibrated for three phenolic acids. Linearity was obtained in the concentration range 0.1-1.0muM caffeic acid, 0.05-0.2muM ferulic acid, 2.0-14.0muM syringic acid for laccase immobilised on a commercial oxygen electrode and 2.0-30.0muM caffeic acid, 2.0-10.0muM ferulic acid, 4.0-30.0muM syringic acid for laccase immobilised on ferrocene-modified screen-printed electrodes. Furthermore, optimal pH, temperature and thermal stability studies were performed with the commercial oxygen electrode. Both electrodes were used for determination of a class of phenolic acids, achieving a cheap and fast tool and an easy to be used procedure for screening real samples of human plasma.

0 Followers
 · 
262 Views
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Herein, a mediated Gluconobacter oxydans biosensor was constructed by immobilizing the intact cells on the modified gold electrode. The surface was initially modified with gold nanoparticles and then, self-assembled monolayers were formed by using 6-(ferrocenyl) hexanethiol. Finally, G. oxydans cells were adsorbed onto the surfaces and the bio-active layer was covered with a dialysis membrane. As well as the response characteristics, stabilities and substrate specificities ere investigated.
    Electroanalysis 10/2014; 27(1). DOI:10.1002/elan.201400371 · 2.50 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Studies were carried on the decolorization of the textile dye reactive blue 19 (RB 19) by a novel isolate of Coprinus plicatilis (C. plicatilis) fungi. We describe an in vitro optimization process for decolorization and its behavior under different conditions of carbon and nitrogen sources, pH, temperature and substrate concentration. The optimal conditions for decolorization were obtained in media containing intermediate concentrations of ammonium oxalate and glucose (10 g/L) as nitrogen and carbon sources, respectively, at 26[degree sign]C and pH = 5.5. Maximum decolorization efficiency against RB 19 achieved in this study was around 99%. Ultra-violet and visible (UV-vis) spectrophotometric analyses, before and after decolorization, suggest that decolorization was due to biodegradation. This effect was associated with laccase enzyme displaying good tolerance to a wide range of pH values, salt concentrations and temperatures, suggesting a potential role for this organism in the remediation of real dye containing effluents. In conclusion, laccase activity in C. plicatilis was firstly described in this study.
    Journal of Environmental Health Science and Engineering 02/2014; 12(1):49. DOI:10.1186/2052-336X-12-49 · 1.01 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Typically, the use of heterogeneous enzyme catalysis is aimed at sustainability, reusability, or enhanced functionality of the biocatalyst and is achieved by immobilizing enzymes onto a support matrix or at a defined interface. Controlled enzyme immobilization is particularly important in bioelectrocatalysis because the catalyst must be effectively connected to a transducer to exploit its activity. This Review discusses what must be addressed for coupling biocatalysts to an electrode and the toolbox of methods that are available for achieving this outcome. As an illustration, we focus on the immobilization and stabilization of laccases at electronic interfaces. Historically, laccases have been used for the decolorization of dyes and for the synthesis of bio‐organic compounds; however, more recently, they have been applied to the fields of sensing and energy harvesting.1–3 There is an ever‐increasing focus on the development of new energy technologies, in which laccases find application (e.g., as cathodic catalysts in enzymatic fuel cells). Herein, we discuss the heterogeneous laccase biocatalysts that have been reported over the past 10–15 years and discuss why laccases continue to be biotechnologically relevant enzymes. Various methods for the immobilization of laccases are described, including the use of nanoscale supports and a range of encapsulation and cross‐linking chemistries. We consider the application of immobilized laccases to the food industry, in the synthesis of pharmaceuticals, and in environmental applications, specifically in cases in which stabilization through heterogenization of the enzyme is critical to the application. We also include a consideration of electrochemical biosensors and the specific incorporation of laccases on the surfaces of transducers.
    ChemCatChem 06/2013; 5(1). DOI:10.1002/cctc.201200611 · 5.04 Impact Factor

Full-text

Download
88 Downloads
Available from
May 27, 2014