Activity of free and immobilized glucose oxidase

An electrochemical study

Michael J. Danilich, Dominic F Gervasio, Roger E. Marchant

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The activity of free and immobilized glucose oxidase was determined using a sandwich type thin-layer electrochemical cell. The thin-layer cell consisted of a gold electrode deposited on a glass microscope slide, 165 μm thick Teflon TFE spacers, and a glass cover. Enzyme activity was determined by using cyclic voltammetry to measure the amount of hydrogen peroxide produced in the glucose oxidase catalyzed redox reaction between glucose and oxygen in the thin-layer cell. The specific activity of 13.4 nM glucose oxidase in 0.2 M aqueous sodium phosphate, pH 5.2 at room temperature, was calculated to be 4.34 U/mg GOx. Under the same experimental conditions, qualitative detection of the activity of glucose oxidase covalently immobolized to a thin radiofrequency plasma modified poly(etherurethaneurea) film was demonstrated.

Original languageEnglish (US)
Pages (from-to)655-668
Number of pages14
JournalAnnals of Biomedical Engineering
Volume21
Issue number6
DOIs
StatePublished - Nov 1993
Externally publishedYes

Fingerprint

Glucose oxidase
Glass
Electrochemical cells
Redox reactions
Enzyme activity
Polytetrafluoroethylenes
Hydrogen peroxide
Cyclic voltammetry
Glucose
Phosphates
Microscopes
Gold
Sodium
Plasmas
Electrodes
Oxygen
Temperature

Keywords

  • Activity
  • Immobilization
  • Plasma polymer

ASJC Scopus subject areas

  • Biomedical Engineering

Cite this

Activity of free and immobilized glucose oxidase : An electrochemical study. / Danilich, Michael J.; Gervasio, Dominic F; Marchant, Roger E.

In: Annals of Biomedical Engineering, Vol. 21, No. 6, 11.1993, p. 655-668.

Research output: Contribution to journalArticle

Danilich, Michael J. ; Gervasio, Dominic F ; Marchant, Roger E. / Activity of free and immobilized glucose oxidase : An electrochemical study. In: Annals of Biomedical Engineering. 1993 ; Vol. 21, No. 6. pp. 655-668.
@article{7d772c667140402ea3fa93bc46845a83,
title = "Activity of free and immobilized glucose oxidase: An electrochemical study",
abstract = "The activity of free and immobilized glucose oxidase was determined using a sandwich type thin-layer electrochemical cell. The thin-layer cell consisted of a gold electrode deposited on a glass microscope slide, 165 μm thick Teflon TFE spacers, and a glass cover. Enzyme activity was determined by using cyclic voltammetry to measure the amount of hydrogen peroxide produced in the glucose oxidase catalyzed redox reaction between glucose and oxygen in the thin-layer cell. The specific activity of 13.4 nM glucose oxidase in 0.2 M aqueous sodium phosphate, pH 5.2 at room temperature, was calculated to be 4.34 U/mg GOx. Under the same experimental conditions, qualitative detection of the activity of glucose oxidase covalently immobolized to a thin radiofrequency plasma modified poly(etherurethaneurea) film was demonstrated.",
keywords = "Activity, Immobilization, Plasma polymer",
author = "Danilich, {Michael J.} and Gervasio, {Dominic F} and Marchant, {Roger E.}",
year = "1993",
month = "11",
doi = "10.1007/BF02368645",
language = "English (US)",
volume = "21",
pages = "655--668",
journal = "Annals of Biomedical Engineering",
issn = "0090-6964",
publisher = "Springer Netherlands",
number = "6",

}

TY - JOUR

T1 - Activity of free and immobilized glucose oxidase

T2 - An electrochemical study

AU - Danilich, Michael J.

AU - Gervasio, Dominic F

AU - Marchant, Roger E.

PY - 1993/11

Y1 - 1993/11

N2 - The activity of free and immobilized glucose oxidase was determined using a sandwich type thin-layer electrochemical cell. The thin-layer cell consisted of a gold electrode deposited on a glass microscope slide, 165 μm thick Teflon TFE spacers, and a glass cover. Enzyme activity was determined by using cyclic voltammetry to measure the amount of hydrogen peroxide produced in the glucose oxidase catalyzed redox reaction between glucose and oxygen in the thin-layer cell. The specific activity of 13.4 nM glucose oxidase in 0.2 M aqueous sodium phosphate, pH 5.2 at room temperature, was calculated to be 4.34 U/mg GOx. Under the same experimental conditions, qualitative detection of the activity of glucose oxidase covalently immobolized to a thin radiofrequency plasma modified poly(etherurethaneurea) film was demonstrated.

AB - The activity of free and immobilized glucose oxidase was determined using a sandwich type thin-layer electrochemical cell. The thin-layer cell consisted of a gold electrode deposited on a glass microscope slide, 165 μm thick Teflon TFE spacers, and a glass cover. Enzyme activity was determined by using cyclic voltammetry to measure the amount of hydrogen peroxide produced in the glucose oxidase catalyzed redox reaction between glucose and oxygen in the thin-layer cell. The specific activity of 13.4 nM glucose oxidase in 0.2 M aqueous sodium phosphate, pH 5.2 at room temperature, was calculated to be 4.34 U/mg GOx. Under the same experimental conditions, qualitative detection of the activity of glucose oxidase covalently immobolized to a thin radiofrequency plasma modified poly(etherurethaneurea) film was demonstrated.

KW - Activity

KW - Immobilization

KW - Plasma polymer

UR - http://www.scopus.com/inward/record.url?scp=0027692781&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027692781&partnerID=8YFLogxK

U2 - 10.1007/BF02368645

DO - 10.1007/BF02368645

M3 - Article

VL - 21

SP - 655

EP - 668

JO - Annals of Biomedical Engineering

JF - Annals of Biomedical Engineering

SN - 0090-6964

IS - 6

ER -