Details
| Original language | English |
|---|---|
| Pages (from-to) | 39-44 |
| Number of pages | 6 |
| Journal | Journal of biotechnology |
| Volume | 36 |
| Issue number | 1 |
| Publication status | Published - 29 Jul 1994 |
| Externally published | Yes |
Abstract
A fluorometric fiber-optic biosensor was used to determine the content of glucose and fructose according to the measurement principle of flow injection analysis (FIA). The enzyme glucose-fructose-oxidoreductase (GFOR) isolated from Zymomonas mobilis was confined in a measurement cell behind an ultrafiltration membrane. The GFOR catalyzes the oxidation of glucose to gluconolactone and the reduction of fructose to sorbitol according to the ping-pong mechanism. This unique enzyme contains NADPH tightly confined in the enzyme complex. The change of NADPH fluorescence was detected by a fluorosensor. The stability could be increased remarkably by crosslinking with glutaraldehyde. The detection range for glucose was within a concentration range of 0.055-55.5 mM and that for fructose within 0.278-331 mM. The response time for glucose and fructose was in the range of 40 s and 1 min, respectively. Steady-state was achieved for glucose injection in 2 min and fructose injection in 6.5 min. Sampling time for glucose could be reduced to 37% by including fructose in excess to the sample. This also makes the regenerating step unnecessary. The specificity of this biosensor was tested for different sugars. The results showed that this biosensor system is highly specific, sensitive and suitable for dual analysis of glucose and fructose.
Keywords
- FIA, Fiber-optic biosensor, Glucose-fructose-oxidoreductase, NADPH-dependent fluorescence
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Journal of biotechnology, Vol. 36, No. 1, 29.07.1994, p. 39-44.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A fluorometric fiber-optic biosensor for dual analysis of glucose and fructose using glucose-fructose-oxidoreductase isolated from Zymomonas mobilis
AU - Lee, Sei Jin
AU - Saleemuddin, Mohammed
AU - Scheper, Thomas
AU - Loos, Heidi
AU - Sahm, Hermann
PY - 1994/7/29
Y1 - 1994/7/29
N2 - A fluorometric fiber-optic biosensor was used to determine the content of glucose and fructose according to the measurement principle of flow injection analysis (FIA). The enzyme glucose-fructose-oxidoreductase (GFOR) isolated from Zymomonas mobilis was confined in a measurement cell behind an ultrafiltration membrane. The GFOR catalyzes the oxidation of glucose to gluconolactone and the reduction of fructose to sorbitol according to the ping-pong mechanism. This unique enzyme contains NADPH tightly confined in the enzyme complex. The change of NADPH fluorescence was detected by a fluorosensor. The stability could be increased remarkably by crosslinking with glutaraldehyde. The detection range for glucose was within a concentration range of 0.055-55.5 mM and that for fructose within 0.278-331 mM. The response time for glucose and fructose was in the range of 40 s and 1 min, respectively. Steady-state was achieved for glucose injection in 2 min and fructose injection in 6.5 min. Sampling time for glucose could be reduced to 37% by including fructose in excess to the sample. This also makes the regenerating step unnecessary. The specificity of this biosensor was tested for different sugars. The results showed that this biosensor system is highly specific, sensitive and suitable for dual analysis of glucose and fructose.
AB - A fluorometric fiber-optic biosensor was used to determine the content of glucose and fructose according to the measurement principle of flow injection analysis (FIA). The enzyme glucose-fructose-oxidoreductase (GFOR) isolated from Zymomonas mobilis was confined in a measurement cell behind an ultrafiltration membrane. The GFOR catalyzes the oxidation of glucose to gluconolactone and the reduction of fructose to sorbitol according to the ping-pong mechanism. This unique enzyme contains NADPH tightly confined in the enzyme complex. The change of NADPH fluorescence was detected by a fluorosensor. The stability could be increased remarkably by crosslinking with glutaraldehyde. The detection range for glucose was within a concentration range of 0.055-55.5 mM and that for fructose within 0.278-331 mM. The response time for glucose and fructose was in the range of 40 s and 1 min, respectively. Steady-state was achieved for glucose injection in 2 min and fructose injection in 6.5 min. Sampling time for glucose could be reduced to 37% by including fructose in excess to the sample. This also makes the regenerating step unnecessary. The specificity of this biosensor was tested for different sugars. The results showed that this biosensor system is highly specific, sensitive and suitable for dual analysis of glucose and fructose.
KW - FIA
KW - Fiber-optic biosensor
KW - Glucose-fructose-oxidoreductase
KW - NADPH-dependent fluorescence
UR - http://www.scopus.com/inward/record.url?scp=0027982263&partnerID=8YFLogxK
U2 - 10.1016/0168-1656(94)90021-3
DO - 10.1016/0168-1656(94)90021-3
M3 - Article
AN - SCOPUS:0027982263
VL - 36
SP - 39
EP - 44
JO - Journal of biotechnology
JF - Journal of biotechnology
SN - 0168-1656
IS - 1
ER -