A highly sensitive flow-through amperometric immunosensor based on the peroxidase chip and enzyme-channeling principle
(2003) In Biosensors & Bioelectronics 18(11). p.1321-1327- Abstract
- A concept based on the Peroxidase-chip (P-chip), antibody co-immobilization, competitive and enzyme-channeling principle was exploited to develop an integrated flow-through amperometric biosensor for detection of environmental pollutants such as s-triazine herbicides. In this concept, recombinant peroxidase is immobilized on the gold electrode (P-chip) in such a way that direct electron transfer is achieved. The recognition and quantitation the target analyte is realized through the competition between the simazine-glucose oxidase (GOD) conjugate and free simazine for the binding sites of the monoclonal antibody co-immobilized with peroxidase on the gold electrode. The arrangement allows to generate a specific signal in the presence of... (More)
- A concept based on the Peroxidase-chip (P-chip), antibody co-immobilization, competitive and enzyme-channeling principle was exploited to develop an integrated flow-through amperometric biosensor for detection of environmental pollutants such as s-triazine herbicides. In this concept, recombinant peroxidase is immobilized on the gold electrode (P-chip) in such a way that direct electron transfer is achieved. The recognition and quantitation the target analyte is realized through the competition between the simazine-glucose oxidase (GOD) conjugate and free simazine for the binding sites of the monoclonal antibody co-immobilized with peroxidase on the gold electrode. The arrangement allows to generate a specific signal in the presence of glucose through the channeling of H2O2 produced by GOD conjugate bound to the antibody. The immunosensor exhibited 50% signal decrease (IC50 value) at aproximately 0.02 mug l(-1). A concentration of 0.1 ng l(-1) gave a signal clearly distinguishable from the blank whereas the ELISA using the same antibody had a typical detection limit of about 1 mug l(-1), which is four orders of magnitude higher compared to the presented biosensor system. The results demonstrated that gene engineering biomolecules, in this case recombinant peroxidase, might be attractive reagents for the development of electrochemical immunosensors. (C) 2003 Elsevier Science B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/301781
- author
- Zeravik, J ; Ruzgas, Tautgirdas LU and Franek, M
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- glucose oxidase, recombinant peroxidase, co-immobilization, antibody, enzyme-channeling, immunosensor
- in
- Biosensors & Bioelectronics
- volume
- 18
- issue
- 11
- pages
- 1321 - 1327
- publisher
- Elsevier
- external identifiers
-
- pmid:12896832
- wos:000185193500002
- scopus:0042706515
- ISSN
- 1873-4235
- DOI
- 10.1016/S0956-5663(03)00076-9
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
- id
- 7c09dab4-0679-4a10-8266-a96428930ca4 (old id 301781)
- date added to LUP
- 2016-04-01 16:54:14
- date last changed
- 2022-01-28 23:01:06
@article{7c09dab4-0679-4a10-8266-a96428930ca4,
abstract = {{A concept based on the Peroxidase-chip (P-chip), antibody co-immobilization, competitive and enzyme-channeling principle was exploited to develop an integrated flow-through amperometric biosensor for detection of environmental pollutants such as s-triazine herbicides. In this concept, recombinant peroxidase is immobilized on the gold electrode (P-chip) in such a way that direct electron transfer is achieved. The recognition and quantitation the target analyte is realized through the competition between the simazine-glucose oxidase (GOD) conjugate and free simazine for the binding sites of the monoclonal antibody co-immobilized with peroxidase on the gold electrode. The arrangement allows to generate a specific signal in the presence of glucose through the channeling of H2O2 produced by GOD conjugate bound to the antibody. The immunosensor exhibited 50% signal decrease (IC50 value) at aproximately 0.02 mug l(-1). A concentration of 0.1 ng l(-1) gave a signal clearly distinguishable from the blank whereas the ELISA using the same antibody had a typical detection limit of about 1 mug l(-1), which is four orders of magnitude higher compared to the presented biosensor system. The results demonstrated that gene engineering biomolecules, in this case recombinant peroxidase, might be attractive reagents for the development of electrochemical immunosensors. (C) 2003 Elsevier Science B.V. All rights reserved.}},
author = {{Zeravik, J and Ruzgas, Tautgirdas and Franek, M}},
issn = {{1873-4235}},
keywords = {{glucose oxidase; recombinant peroxidase; co-immobilization; antibody; enzyme-channeling; immunosensor}},
language = {{eng}},
number = {{11}},
pages = {{1321--1327}},
publisher = {{Elsevier}},
series = {{Biosensors & Bioelectronics}},
title = {{A highly sensitive flow-through amperometric immunosensor based on the peroxidase chip and enzyme-channeling principle}},
url = {{http://dx.doi.org/10.1016/S0956-5663(03)00076-9}},
doi = {{10.1016/S0956-5663(03)00076-9}},
volume = {{18}},
year = {{2003}},
}