Phenol biosensor based on Sonogel-Carbon transducer with tyrosinase alumina sol–gel immobilization

Zejli, Hanane; Cisneros, José Luis; Naranjo-Rodrı́guez, Ignacio; Liu, Baohong; Temsamani, Khalid Riffi; Marty, Jean‐Louis

doi:10.1016/j.aca.2008.02.029

Cited by 59 publications

(21 citation statements)

References 19 publications

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“…The stability of covalent binding is superior to other methods such as sol-gel, physical adsorption. [49][50][51][52] In this study, we constructed a novel electrochemical tyrosinase biosensor by determination of catechol based on Tyrosinase (TYR)/ Glutaraldehyde (GA)/poly(Thionine) (pTN) modified glassy carbon electrode (GCE). The electropolymerized thionine onto the GC surface donated terminal amino group for the coupling reagent, in this case, glutaraldehyde.…”

Section: Introductionmentioning

confidence: 99%

Tyrosinase Modified Poly(thionine) Electrodeposited Glassy Carbon Electrode for Amperometric Determination of Catechol

Wang

Zhang

et al. 2017

Electrochemistry

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A stepwise strategy of mediator-free amperometric biosensor for the detection of catechol was developed based on the covalent bonding of tyrosinase (TYR) onto thionine (TN)-electrodeposited glassy carbon (GC) surface via glutaraldehyde (GA). Prior to the TYR-immobilization, poly(thionine) was prepared on a GC electrode surface by an electrooxidative polymerization of thionine. The TYR/GA/pTN modified electrode was evaluated by SEM and EIS measurements. The terminal amino groups (-NH 2 ) which electrodeposited on the GC surface were cross-linked with protein lysine group (or cysteine group) by GA. The resulting TYR/GA/pTN-immobilized GCE was utilized as a working electrode unit of a catechol-detect biosensor. Catechol was used as model analyte for the evaluation of catecholase activity, and the signal based on the electro-reduction of the enzymatically produced o-quinone species were monitored at −0.05 V vs. Ag/AgCl. The resulting TYR/GA/pTN/GCE biosensor exhibited rapid and sensitive response to catechol (100% response time: ≈5 s, sensitivity: 5.04 µA/mM, detection limit: 6.0 µM. The TYR/GA/ pTN/GCE retained 71% of original activity for catechol oxidation after 1 month storage.

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Section: Introductionmentioning

confidence: 99%

Tyrosinase Modified Poly(thionine) Electrodeposited Glassy Carbon Electrode for Amperometric Determination of Catechol

Wang

Zhang

et al. 2017

Electrochemistry

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“…6 Moreover, the possibility to immobilize tyrosinase on stable and low cost supports further increase the interest for this enzyme in industrial applications. 7 Examples of the immobilization of tyrosinase on carbon nanotube, 8 copolymer matrices, 9 chitosan, 10 gold nanoparticles, 11 alumina sol-gel, 12 membrane alginate, polyacrylamide, and gelatine gels 13 have been reported in the production of L-dopa, 14 in the removal of phenolic compounds from waste water, 15 and in other industrial applications. 16 However, some of these immobilization methods are rather complicated and do not give good enzyme stability or retention.…”

Section: Introductionmentioning

confidence: 99%

Layer-by-Layer coated tyrosinase: An efficient and selective synthesis of catechols

Guazzaroni

Crestini

Saladino

2012

Bioorganic & Medicinal Chemistry

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a b s t r a c tAgaricus bisporous tyrosinase was immobilized on commercial available epoxy-resin Eupergit Ò C250L and then coated by the Layer-by-Layer method (LbL). The two novel heterogeneous biocatalysts were characterized for their morphology, pH and storage stability, kinetic properties (K m , V max , V max /K m ) and reusability. These biocatalysts were used for the efficient and selective synthesis of bioactive catechols under mild and environmental friendly experimental conditions. Ascorbic acid was added in the reaction medium to inhibit the formation of ortho-quinones, thus avoiding the known enzyme suicide inactivation process. Catechols were obtained mostly in quantitative yields and conversion of substrate. Tyrosinase immobilized on Eupergit Ò C250L and coated by the LbL method showed better catalytic activities, higher pH and storage stability, and reusability with respect to immobilized uncoated tyrosinase. Since chemical procedures to synthesize catechols are often expensive and with high environmental impact, the use of immobilized tyrosinase represents an efficient alternative for the preparation of this family of bioactive compounds.

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“…At present, an electrochemical biosensor has been proven to be an accurate and versatile analytical method for the detection of phenolic compounds, due to such advantages as high selectivity, relatively low cost, and the miniaturization and automation. [1][2][3] More recently, various supporting materials, such as graphite composite, 4 conducting polymer, 5,6 sol-gel films, 7,8 and self-assembled monolayers (SAMs), 9 have been successfully utilized to immobilize enzymes for the construction of a tyrosinase (tyr)-based electrochemical biosensor. Among them, sol-gel film offers a better biointerface for the immobilization of enzymes.…”

Section: Introductionmentioning

confidence: 99%

Gold Nanoparticles-Enhanced Amperometric Tyrosinase Biosensor Based on Three-Dimensional Sol-Gel Film-Modified Gold Electrodes

Ren

Wang

et al. 2013

ANAL. SCI.

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Phenol biosensor based on Sonogel-Carbon transducer with tyrosinase alumina sol–gel immobilization

Cited by 59 publications

References 19 publications

Tyrosinase Modified Poly(thionine) Electrodeposited Glassy Carbon Electrode for Amperometric Determination of Catechol

Tyrosinase Modified Poly(thionine) Electrodeposited Glassy Carbon Electrode for Amperometric Determination of Catechol

Layer-by-Layer coated tyrosinase: An efficient and selective synthesis of catechols

Gold Nanoparticles-Enhanced Amperometric Tyrosinase Biosensor Based on Three-Dimensional Sol-Gel Film-Modified Gold Electrodes

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