Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds

J. Cortez; E. Vorobieva; D. Gralheira; I. Osório; L. Soares; N. Vale; E. Pereira; P. Gomes; R. Franco

doi:10.1007/s11051-010-0099-8

Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds

J. Cortez^*, E. Vorobieva, D. Gralheira, I. Osório, L. Soares, N. Vale, E. Pereira, P. Gomes, R. Franco

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

Bionanoconjugates of the enzyme tyrosinase (TYR) and gold nanoparticles (AuNPs) functionalised with a peptide (CALNN) were produced in solution and characterised. The formation of stable TYR-AuNP:CALNN bionanoconjugates (BNCs) was supported by a decrease of the surface charge of the BNCs as determined by ζ-potential and an increase in hydrodynamic diameter as determined by Dynamic Light Scattering (DLS). UV/Vis studies of pH-induced aggregation revealed distinct protonation patterns for the BNCs when compared with AuNP:CALNN alone, further substantiating BNC formation. Activity studies of the BNCs for the reduction of di-phenols in solution indicated that TYR not only remains active after conjugation, but interestingly its activity in the BNCs is higher than for the free enzyme. In conclusion, AuNP:CALNN can provide a suitable platform for the immobilisation of TYR, leading to BNCs with increased enzyme activity and a wider pH working range, with promising uses in electrochemical biosensors for the detection of mono- and di-phenolic compounds.

Original language	English
Pages (from-to)	1101-1113
Number of pages	13
Journal	Journal of Nanoparticle Research
Volume	13
Issue number	3
DOIs	https://doi.org/10.1007/s11051-010-0099-8
Publication status	Published - Mar 2011
Externally published	Yes

Keywords

Bionanoconjugate
Biosensor
Environmental pollutants
Gold nanoparticle
Tyrosinase

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10.1007/s11051-010-0099-8

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title = "Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds",

abstract = "Bionanoconjugates of the enzyme tyrosinase (TYR) and gold nanoparticles (AuNPs) functionalised with a peptide (CALNN) were produced in solution and characterised. The formation of stable TYR-AuNP:CALNN bionanoconjugates (BNCs) was supported by a decrease of the surface charge of the BNCs as determined by ζ-potential and an increase in hydrodynamic diameter as determined by Dynamic Light Scattering (DLS). UV/Vis studies of pH-induced aggregation revealed distinct protonation patterns for the BNCs when compared with AuNP:CALNN alone, further substantiating BNC formation. Activity studies of the BNCs for the reduction of di-phenols in solution indicated that TYR not only remains active after conjugation, but interestingly its activity in the BNCs is higher than for the free enzyme. In conclusion, AuNP:CALNN can provide a suitable platform for the immobilisation of TYR, leading to BNCs with increased enzyme activity and a wider pH working range, with promising uses in electrochemical biosensors for the detection of mono- and di-phenolic compounds.",

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AU - Cortez, J.

AU - Vorobieva, E.

AU - Gralheira, D.

AU - Osório, I.

AU - Soares, L.

AU - Vale, N.

AU - Pereira, E.

AU - Gomes, P.

AU - Franco, R.

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N2 - Bionanoconjugates of the enzyme tyrosinase (TYR) and gold nanoparticles (AuNPs) functionalised with a peptide (CALNN) were produced in solution and characterised. The formation of stable TYR-AuNP:CALNN bionanoconjugates (BNCs) was supported by a decrease of the surface charge of the BNCs as determined by ζ-potential and an increase in hydrodynamic diameter as determined by Dynamic Light Scattering (DLS). UV/Vis studies of pH-induced aggregation revealed distinct protonation patterns for the BNCs when compared with AuNP:CALNN alone, further substantiating BNC formation. Activity studies of the BNCs for the reduction of di-phenols in solution indicated that TYR not only remains active after conjugation, but interestingly its activity in the BNCs is higher than for the free enzyme. In conclusion, AuNP:CALNN can provide a suitable platform for the immobilisation of TYR, leading to BNCs with increased enzyme activity and a wider pH working range, with promising uses in electrochemical biosensors for the detection of mono- and di-phenolic compounds.

AB - Bionanoconjugates of the enzyme tyrosinase (TYR) and gold nanoparticles (AuNPs) functionalised with a peptide (CALNN) were produced in solution and characterised. The formation of stable TYR-AuNP:CALNN bionanoconjugates (BNCs) was supported by a decrease of the surface charge of the BNCs as determined by ζ-potential and an increase in hydrodynamic diameter as determined by Dynamic Light Scattering (DLS). UV/Vis studies of pH-induced aggregation revealed distinct protonation patterns for the BNCs when compared with AuNP:CALNN alone, further substantiating BNC formation. Activity studies of the BNCs for the reduction of di-phenols in solution indicated that TYR not only remains active after conjugation, but interestingly its activity in the BNCs is higher than for the free enzyme. In conclusion, AuNP:CALNN can provide a suitable platform for the immobilisation of TYR, leading to BNCs with increased enzyme activity and a wider pH working range, with promising uses in electrochemical biosensors for the detection of mono- and di-phenolic compounds.

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Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds

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Keywords

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