Enzyme electrode for on-line determination of ethanol and methanol
Journal Article
·
· Biotechnol. Bioeng.; (United States)
Since a stable alcohol oxidase with a high specific activity is not commercially available, they propose to produce and purify this enzyme from a strain of the yeast Hansenula polymorpha. This alcohol oxidase was immobilized into a gelatin matrix and its activity was estimated by a pO/sub 2/ sensor. The enzyme electrode obtained was then used in a continuous flow system to measure methanol or ethanol concentrations. The sample oxygen content dependence of the signal was minimized by the support properties. Measuring time for each sample were less than two minutes including response data treatment and rinsing step. The enzyme electrode response was set for ethanol from 0.5 mM to 15 mM and for methanol from 10 mM to 300 mM. On repeated use, the electrode signal for 10 mM of ethanol was stable for at least 500 assays. Analysis have been performed in different beverages such as wine and beer, and the results compared to those obtained with classical methods of analysis.
- Research Organization:
- Universite de Technologie de Compiegne (France)
- OSTI ID:
- 7015389
- Journal Information:
- Biotechnol. Bioeng.; (United States), Journal Name: Biotechnol. Bioeng.; (United States) Vol. 30:9; ISSN BIBIA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
09 BIOMASS FUELS
090222* -- Alcohol Fuels-- Preparation from Wastes or Biomass-- (1976-1989)
ALCOHOLS
ELECTRODES
ENZYME ACTIVITY
ENZYMES
ETHANOL
FRACTIONATION
FUNGI
HYDROXY COMPOUNDS
IMMOBILIZED ENZYMES
METHANOL
MICROORGANISMS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PLANTS
SEPARATION PROCESSES
YEASTS
YIELDS
090222* -- Alcohol Fuels-- Preparation from Wastes or Biomass-- (1976-1989)
ALCOHOLS
ELECTRODES
ENZYME ACTIVITY
ENZYMES
ETHANOL
FRACTIONATION
FUNGI
HYDROXY COMPOUNDS
IMMOBILIZED ENZYMES
METHANOL
MICROORGANISMS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PLANTS
SEPARATION PROCESSES
YEASTS
YIELDS