PMID- 3454651
OWN - NLM
STAT- MEDLINE
DCOM- 19880912
LR  - 20191029
IS  - 0265-928X (Print)
IS  - 0265-928X (Linking)
VI  - 2
IP  - 2
DP  - 1986
TI  - Quinoprotein glucose dehydrogenase and its application in an amperometric glucose 
      sensor.
PG  - 71-87
AB  - Glucose dehydrogenase (GDH), one of the recently discovered NAD(P)+-independent 
      'quinoprotein' class of oxidoreductase enzymes, was purified from Acinetobacter 
      calcoaceticus LMD 79.41 and immobilised on a 1,1'-dimethylferrocene-modified 
      graphite foil electrode. The second-order rate constant (ks) for the transfer of 
      electrons between GDH and ferrocenemonocarboxylic acid (FMCA) in a homogeneous 
      system, determined using direct current (DC) cyclic voltammetry, was found to be 
      9.4 x 10(6) litres mol-1 s-1. This value of ks for GDH was more than 40 times 
      greater than that for the flavoprotein glucose oxidase (GOD) under identical 
      conditions. Such high catalytic activities were also observed when GDH was 
      immobilised in the presence of an insoluble ferrocene derivative; a biosensor 
      based on GDH was found to produce more than twice the current density of similar 
      GOD-based electrodes. The steady-state current produced by the GDH-based 
      electrode was limited by the enzymic reaction since methods which increased the 
      enzyme loadings elevated the upper limit of glucose detection from 5 mM to 15 mM. 
      The temperature, pH, stability and response characteristics of the GDH-based 
      glucose sensor illustrate its potential usefulness for a variety of practical 
      applications. In particular, the high catalytic activity and oxygen insensitivity 
      of this biosensor make it suitable for in vivo blood glucose monitoring in the 
      management of diabetes.
FAU - D'Costa, E J
AU  - D'Costa EJ
AD  - Biotechnology Centre, Cranfield Institute of Technology, Bedford, Great Britain.
FAU - Higgins, I J
AU  - Higgins IJ
FAU - Turner, A P
AU  - Turner AP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biosensors
JT  - Biosensors
JID - 8601088
RN  - 0 (Blood Glucose)
RN  - 0 (Enzymes, Immobilized)
RN  - EC 1.1.- (Carbohydrate Dehydrogenases)
RN  - EC 1.1.1.- (Glucose Dehydrogenases)
RN  - EC 1.1.5.2 (glucose dehydrogenase (pyrroloquinoline-quinone))
RN  - IY9XDZ35W2 (Glucose)
SB  - IM
MH  - Acinetobacter/*enzymology
MH  - Blood Glucose/*analysis
MH  - Carbohydrate Dehydrogenases/*metabolism
MH  - Chromatography, High Pressure Liquid/methods
MH  - Electrochemistry/instrumentation/methods
MH  - Enzymes, Immobilized/*metabolism
MH  - Glucose/*analysis
MH  - Glucose Dehydrogenases/isolation & purification/*metabolism
MH  - Humans
MH  - Monitoring, Physiologic/methods
EDAT- 1986/01/01 00:00
MHDA- 1986/01/01 00:01
CRDT- 1986/01/01 00:00
PHST- 1986/01/01 00:00 [pubmed]
PHST- 1986/01/01 00:01 [medline]
PHST- 1986/01/01 00:00 [entrez]
AID - 10.1016/0265-928x(86)80011-6 [doi]
PST - ppublish
SO  - Biosensors. 1986;2(2):71-87. doi: 10.1016/0265-928x(86)80011-6.