A novel ISFET-based NAD+-dependent enzyme sensor for lactate

Andrei B. Kharitonov; Maya Zayats; Lital Alfonta; Eugenii Katz; Itamar Willner

doi:10.1016/S0925-4005(01)00640-2

A novel ISFET-based NAD⁺-dependent enzyme sensor for lactate

Andrei B. Kharitonov, Maya Zayats, Lital Alfonta, Eugenii Katz, Itamar Willner

Research output: Contribution to journal › Conference article › peer-review

49 Scopus citations

Abstract

An integrated NAD⁺-dependent enzyme field-effect transistor (ENFET) device for the biosensing of lactate is described. The aminosiloxane-functionalized gate interface is modified with pyrroloquinoline quinone (PQQ) that acts as a catalyst for the oxidation of NADH. A synthetic amino-derivative of NAD⁺ is covalently linked to the PQQ monolayer. Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interaction between NAD⁺-dependent enzyme, lactate dehydrogenase (LDH) (E.C. 1.1.1.27), and the NAD⁺-functionalized Au-electrode surface. The association constant of 1.5 × 10⁵ M^-1 was found by both techniques. The affinity complex formed between the NAD⁺/PQQ-assembly and the LDH is cross-linked and yields an integrated biosensor ENFET-device for the analysis of lactate. The device reveals the lower detection limit of 1 × 10^-4 M for lactate and the sensitivity of 24 ± 2 mV dec^-1. The response time of the device is as low as 15 s.

Original language	English
Pages (from-to)	203-210
Number of pages	8
Journal	Sensors and Actuators, B: Chemical
Volume	76
Issue number	1-3
DOIs	https://doi.org/10.1016/S0925-4005(01)00640-2
State	Published - 1 Jun 2001
Externally published	Yes
Event	Proceeding of the 8th International Meeting on Chemical Sensors - Basel, Switzerland Duration: 2 Jul 2000 → 5 Jul 2000

Keywords

Biosensor
Chronopotentiometry
ENFET
Field-effect transistor
ISFET
Impedance spectroscopy
Lactate
NAD-dependent enzyme
PQQ
Pyrroloquinoline quinone

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Instrumentation
Condensed Matter Physics
Surfaces, Coatings and Films
Metals and Alloys
Electrical and Electronic Engineering
Materials Chemistry

Access to Document

10.1016/S0925-4005(01)00640-2

Cite this

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title = "A novel ISFET-based NAD+-dependent enzyme sensor for lactate",

abstract = "An integrated NAD+-dependent enzyme field-effect transistor (ENFET) device for the biosensing of lactate is described. The aminosiloxane-functionalized gate interface is modified with pyrroloquinoline quinone (PQQ) that acts as a catalyst for the oxidation of NADH. A synthetic amino-derivative of NAD+ is covalently linked to the PQQ monolayer. Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interaction between NAD+-dependent enzyme, lactate dehydrogenase (LDH) (E.C. 1.1.1.27), and the NAD+-functionalized Au-electrode surface. The association constant of 1.5 × 105 M-1 was found by both techniques. The affinity complex formed between the NAD+/PQQ-assembly and the LDH is cross-linked and yields an integrated biosensor ENFET-device for the analysis of lactate. The device reveals the lower detection limit of 1 × 10-4 M for lactate and the sensitivity of 24 ± 2 mV dec-1. The response time of the device is as low as 15 s.",

keywords = "Biosensor, Chronopotentiometry, ENFET, Field-effect transistor, ISFET, Impedance spectroscopy, Lactate, NAD-dependent enzyme, PQQ, Pyrroloquinoline quinone",

author = "Kharitonov, {Andrei B.} and Maya Zayats and Lital Alfonta and Eugenii Katz and Itamar Willner",

note = "Funding Information: This research is supported by The Israel Ministry of Science as an Infrastructure Project on Biomicroelectronics. L.A. acknowledges the Eshkol fellowship, The Israel Ministry of Science. ; Proceeding of the 8th International Meeting on Chemical Sensors ; Conference date: 02-07-2000 Through 05-07-2000",

year = "2001",

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doi = "10.1016/S0925-4005(01)00640-2",

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pages = "203--210",

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TY - JOUR

T1 - A novel ISFET-based NAD+-dependent enzyme sensor for lactate

AU - Kharitonov, Andrei B.

AU - Zayats, Maya

AU - Alfonta, Lital

AU - Katz, Eugenii

AU - Willner, Itamar

N1 - Funding Information: This research is supported by The Israel Ministry of Science as an Infrastructure Project on Biomicroelectronics. L.A. acknowledges the Eshkol fellowship, The Israel Ministry of Science.

PY - 2001/6/1

Y1 - 2001/6/1

N2 - An integrated NAD+-dependent enzyme field-effect transistor (ENFET) device for the biosensing of lactate is described. The aminosiloxane-functionalized gate interface is modified with pyrroloquinoline quinone (PQQ) that acts as a catalyst for the oxidation of NADH. A synthetic amino-derivative of NAD+ is covalently linked to the PQQ monolayer. Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interaction between NAD+-dependent enzyme, lactate dehydrogenase (LDH) (E.C. 1.1.1.27), and the NAD+-functionalized Au-electrode surface. The association constant of 1.5 × 105 M-1 was found by both techniques. The affinity complex formed between the NAD+/PQQ-assembly and the LDH is cross-linked and yields an integrated biosensor ENFET-device for the analysis of lactate. The device reveals the lower detection limit of 1 × 10-4 M for lactate and the sensitivity of 24 ± 2 mV dec-1. The response time of the device is as low as 15 s.

AB - An integrated NAD+-dependent enzyme field-effect transistor (ENFET) device for the biosensing of lactate is described. The aminosiloxane-functionalized gate interface is modified with pyrroloquinoline quinone (PQQ) that acts as a catalyst for the oxidation of NADH. A synthetic amino-derivative of NAD+ is covalently linked to the PQQ monolayer. Faradaic impedance spectroscopy and chronopotentiometry are used as electrochemical methods for probing in situ bioaffinity interaction between NAD+-dependent enzyme, lactate dehydrogenase (LDH) (E.C. 1.1.1.27), and the NAD+-functionalized Au-electrode surface. The association constant of 1.5 × 105 M-1 was found by both techniques. The affinity complex formed between the NAD+/PQQ-assembly and the LDH is cross-linked and yields an integrated biosensor ENFET-device for the analysis of lactate. The device reveals the lower detection limit of 1 × 10-4 M for lactate and the sensitivity of 24 ± 2 mV dec-1. The response time of the device is as low as 15 s.

KW - Biosensor

KW - Chronopotentiometry

KW - ENFET

KW - Field-effect transistor

KW - ISFET

KW - Impedance spectroscopy

KW - Lactate

KW - NAD-dependent enzyme

KW - PQQ

KW - Pyrroloquinoline quinone

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DO - 10.1016/S0925-4005(01)00640-2

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Y2 - 2 July 2000 through 5 July 2000

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