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Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications.

Risveden, Klas LU ; Dick Thelander, Kimberly LU ; Bhand, Sunil LU ; Rydberg, Patrik; Samuelson, Lars LU and Danielsson, Bengt LU (2010) In Nanotechnology 21(5).
Abstract
A novel lab-on-a-chip nanotree enzyme reactor is demonstrated for the detection of acetylcholine. The reactors are intended for use in the RISFET (regional ion sensitive field effect transistor) nanosensor, and are constructed from gold-tipped branched nanorod structures grown on SiN(x)-covered wafers. Two different reactors are shown: one with simple, one-dimensional nanorods and one with branched nanorod structures (nanotrees). Significantly higher enzymatic activity is found for the nanotree reactors than for the nanorod reactors, most likely due to the increased gold surface area and thereby higher enzyme binding capacity. A theoretical calculation is included to show how the enzyme kinetics and hence the sensitivity can be influenced... (More)
A novel lab-on-a-chip nanotree enzyme reactor is demonstrated for the detection of acetylcholine. The reactors are intended for use in the RISFET (regional ion sensitive field effect transistor) nanosensor, and are constructed from gold-tipped branched nanorod structures grown on SiN(x)-covered wafers. Two different reactors are shown: one with simple, one-dimensional nanorods and one with branched nanorod structures (nanotrees). Significantly higher enzymatic activity is found for the nanotree reactors than for the nanorod reactors, most likely due to the increased gold surface area and thereby higher enzyme binding capacity. A theoretical calculation is included to show how the enzyme kinetics and hence the sensitivity can be influenced and increased by the control of electrical fields in relation to the active sites of enzymes in an electronic biosensor. The possible effects of electrical fields employed in the RISFET on the function of acetylcholine esterase is investigated using quantum chemical methods, which show that the small electric field strengths used are unlikely to affect enzyme kinetics. Acetylcholine esterase activity is determined using choline oxidase and peroxidase by measuring the amount of choline formed using the chemiluminescent luminol reaction. (Less)
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organization
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Contribution to journal
publication status
published
subject
keywords
Biology and Life Sciences, Technology and Engineering, Earth and Environmental Sciences, Chemistry, Medicine and Health Sciences
in
Nanotechnology
volume
21
issue
5
publisher
IOP Publishing
external identifiers
  • wos:000273348400002
  • pmid:20023308
  • scopus:75249089563
ISSN
0957-4484
DOI
10.1088/0957-4484/21/5/055102
language
English
LU publication?
yes
id
e422d8a4-1bd8-45d4-a89e-d8ecb1951919 (old id 1523449)
date added to LUP
2010-01-12 07:57:10
date last changed
2018-05-29 11:22:54
@article{e422d8a4-1bd8-45d4-a89e-d8ecb1951919,
  abstract     = {A novel lab-on-a-chip nanotree enzyme reactor is demonstrated for the detection of acetylcholine. The reactors are intended for use in the RISFET (regional ion sensitive field effect transistor) nanosensor, and are constructed from gold-tipped branched nanorod structures grown on SiN(x)-covered wafers. Two different reactors are shown: one with simple, one-dimensional nanorods and one with branched nanorod structures (nanotrees). Significantly higher enzymatic activity is found for the nanotree reactors than for the nanorod reactors, most likely due to the increased gold surface area and thereby higher enzyme binding capacity. A theoretical calculation is included to show how the enzyme kinetics and hence the sensitivity can be influenced and increased by the control of electrical fields in relation to the active sites of enzymes in an electronic biosensor. The possible effects of electrical fields employed in the RISFET on the function of acetylcholine esterase is investigated using quantum chemical methods, which show that the small electric field strengths used are unlikely to affect enzyme kinetics. Acetylcholine esterase activity is determined using choline oxidase and peroxidase by measuring the amount of choline formed using the chemiluminescent luminol reaction.},
  articleno    = {55102},
  author       = {Risveden, Klas and Dick Thelander, Kimberly and Bhand, Sunil and Rydberg, Patrik and Samuelson, Lars and Danielsson, Bengt},
  issn         = {0957-4484},
  keyword      = {Biology and Life Sciences,Technology and Engineering,Earth and Environmental Sciences,Chemistry,Medicine and Health Sciences},
  language     = {eng},
  number       = {5},
  publisher    = {IOP Publishing},
  series       = {Nanotechnology},
  title        = {Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications.},
  url          = {http://dx.doi.org/10.1088/0957-4484/21/5/055102},
  volume       = {21},
  year         = {2010},
}