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Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing

The possibility of modifying the surface properties of multi-walled carbon nanotubes (MWCNTs) has stimulated increasing interest in their application as components in biosensors. In this sense, it is possible to employ surface modified MWCNTs as support to immobilize biomaterials such as enzymes. In...

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Main Authors: Shahir, Shafinaz, Tai, , Boon Kai, Majid, Zaiton, Buang, Nor Aziah
格式: Article
语言:English
English
出版: Ibnu Sina Institute 2011
主题:
Q Science
在线阅读:http://eprints.utm.my/id/eprint/39792/1/ShafinazShahir2011_CovalentImmobilizationofTyrosinaseontoMulti.Pdf
http://eprints.utm.my/id/eprint/39792/2/160
http://eprints.utm.my/id/eprint/39792/
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spelling my.utm.397922017-10-12T05:20:48Z http://eprints.utm.my/id/eprint/39792/ Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing Shahir, Shafinaz Tai, , Boon Kai Majid, Zaiton Buang, Nor Aziah Q Science The possibility of modifying the surface properties of multi-walled carbon nanotubes (MWCNTs) has stimulated increasing interest in their application as components in biosensors. In this sense, it is possible to employ surface modified MWCNTs as support to immobilize biomaterials such as enzymes. In this study the enzyme tyrosinase was immobilized onto functionalized MWCNTs (fMWCNTs) via covalent bonding and activity of immobilized tyrosinase was measured via electrochemical detection of phenol. MWCNTs were first treated with sulphuric acid and nitric acid with ratio 1 : 3 at 70ºC to introduce carboxylated groups (-COOH). The carboxyl moieties were then activated by treatment with a cross-linker, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) to enable tyrosinase immobilization via amide bonding. FTIR spectra of tyrosinase immobilized fMWCNTs showed the presence of peaks attributing to aliphatic C-N (1382 cm-1) and amide carbonyl (1639 cm-1) vibrations which confirmed successful covalent immobilization of tyrosinase onto fMWCNTs. Electrochemical measurements using tyrosinase-fMWCNTS-CPE revealed increasing limiting current values of reduction peak with increasing phenol concentrations at -200mV. The appearance of the reduction current indicates that the immobilization process retained the biological activity of the covalently bonded tyrosinase on fMWCNTs surface. This study has demonstrated the potential of using MWCNTs as support for enzyme immobilization and their application in biosensor technology. Ibnu Sina Institute 2011-06 Article PeerReviewed application/pdf en http://eprints.utm.my/id/eprint/39792/1/ShafinazShahir2011_CovalentImmobilizationofTyrosinaseontoMulti.Pdf text/html en http://eprints.utm.my/id/eprint/39792/2/160 Shahir, Shafinaz and Tai, , Boon Kai and Majid, Zaiton and Buang, Nor Aziah (2011) Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing. Journal of Fundamental Sciences, 7 (1). pp. 82-88. ISSN 1823-626X
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
language English
English
topic Q Science
spellingShingle Q Science
Shahir, Shafinaz
Tai, , Boon Kai
Majid, Zaiton
Buang, Nor Aziah
Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing
description The possibility of modifying the surface properties of multi-walled carbon nanotubes (MWCNTs) has stimulated increasing interest in their application as components in biosensors. In this sense, it is possible to employ surface modified MWCNTs as support to immobilize biomaterials such as enzymes. In this study the enzyme tyrosinase was immobilized onto functionalized MWCNTs (fMWCNTs) via covalent bonding and activity of immobilized tyrosinase was measured via electrochemical detection of phenol. MWCNTs were first treated with sulphuric acid and nitric acid with ratio 1 : 3 at 70ºC to introduce carboxylated groups (-COOH). The carboxyl moieties were then activated by treatment with a cross-linker, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) to enable tyrosinase immobilization via amide bonding. FTIR spectra of tyrosinase immobilized fMWCNTs showed the presence of peaks attributing to aliphatic C-N (1382 cm-1) and amide carbonyl (1639 cm-1) vibrations which confirmed successful covalent immobilization of tyrosinase onto fMWCNTs. Electrochemical measurements using tyrosinase-fMWCNTS-CPE revealed increasing limiting current values of reduction peak with increasing phenol concentrations at -200mV. The appearance of the reduction current indicates that the immobilization process retained the biological activity of the covalently bonded tyrosinase on fMWCNTs surface. This study has demonstrated the potential of using MWCNTs as support for enzyme immobilization and their application in biosensor technology.
format Article
author Shahir, Shafinaz
Tai, , Boon Kai
Majid, Zaiton
Buang, Nor Aziah
author_facet Shahir, Shafinaz
Tai, , Boon Kai
Majid, Zaiton
Buang, Nor Aziah
author_sort Shahir, Shafinaz
title Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing
title_short Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing
title_full Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing
title_fullStr Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing
title_full_unstemmed Covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing
title_sort covalent immobilization of tyrosinase onto multi-walled carbon nanotube and its potential use in phenol biosensing
publisher Ibnu Sina Institute
publishDate 2011
url http://eprints.utm.my/id/eprint/39792/1/ShafinazShahir2011_CovalentImmobilizationofTyrosinaseontoMulti.Pdf
http://eprints.utm.my/id/eprint/39792/2/160
http://eprints.utm.my/id/eprint/39792/
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score 13.251813

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