A disposable tear glucose biosensor - Part 3: Assessment of enzymatic specificity

Kenneth Lan, Kenyon McAferty, Pankti Shah, Erica Lieberman, Dharmendra R. Patel, Curtiss B. Cook, Jeffrey LaBelle

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Background: A concept for a tear glucose sensor based on amperometric measurement of enzymatic oxidation of glucose was previously presented, using glucose dehydrogenase flavin adenine dinucleotide (GDH-FAD) as the enzyme. Glucose dehydrogenase flavin adenine dinucleotide is further characterized in this article and evaluated for suitability in glucose-sensing applications in purified tear-like saline, with specific attention to the efect of interfering substances only. These interferents are specifically saccharides that could interact with the enzymatic activity seen in the sensor's performance. Methods: Bench top amperometric glucose assays were performed using an assay solution of GDH-FAD and ferricyanide redox mediator with samples of glucose, mannose, lactose, maltose, galactose, fructose, sucrose, and xylose at varying concentrations to evaluate specificity, linear dynamic range, signal size, and signal-to-noise ratio. A comparison study was done by substituting an equivalent activity unit concentration of glucose oxidase (GOx) for GDH-FAD. Results: Glucose dehydrogenase flavin adenine dinucleotide was found to be more sensitive than GOx, producing larger oxidation currents than GOx on an identical glucose concentration gradient, and GDH-FAD exhibited larger slope response (-5.65 × 10-7 versus -3.11 × 10-7 A/mM), signal-to-noise ratio (18.04 versus 2.62), and linear dynamic range (0-30 versus 0-10 mM), and lower background signal (-7.12 versus -261.63 nA) than GOx under the same assay conditions. GDH-FAD responds equally to glucose and xylose but is otherwise specific for glucose. Conclusion: Glucose dehydrogenase flavin adenine dinucleotide compares favorably with GOx in many sensor-relevant attributes and may enable measurement of glucose concentrations both higher and lower than those measurable by GOx. GDH-FAD is a viable enzyme to use in the proposed amperometric tear glucose sensor system and perhaps also in detecting extreme hypoglycemia or hyperglycemia in blood.

Original languageEnglish (US)
Pages (from-to)1108-1115
Number of pages8
JournalJournal of diabetes science and technology
Volume5
Issue number5
DOIs
StatePublished - 2011

Fingerprint

Glucose 1-Dehydrogenase
Flavin-Adenine Dinucleotide
Biosensing Techniques
Tears
Biosensors
Glucose
Glucose Oxidase
Glucose oxidase
Glucose sensors
Assays
Signal-To-Noise Ratio
Signal to noise ratio
Amperometric sensors
Xylose
Oxidation
Maltose
Sensors
Enzymes
Lactose
Mannose

Keywords

  • Biosensor
  • Diabetes mellitus
  • Glucose dehydrogenase flavin adenine dinucleotide
  • Tear glucose monitoring

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Internal Medicine
  • Bioengineering
  • Biomedical Engineering

Cite this

Lan, K., McAferty, K., Shah, P., Lieberman, E., Patel, D. R., Cook, C. B., & LaBelle, J. (2011). A disposable tear glucose biosensor - Part 3: Assessment of enzymatic specificity. Journal of diabetes science and technology, 5(5), 1108-1115. https://doi.org/10.1177/193229681100500511

A disposable tear glucose biosensor - Part 3 : Assessment of enzymatic specificity. / Lan, Kenneth; McAferty, Kenyon; Shah, Pankti; Lieberman, Erica; Patel, Dharmendra R.; Cook, Curtiss B.; LaBelle, Jeffrey.

In: Journal of diabetes science and technology, Vol. 5, No. 5, 2011, p. 1108-1115.

Research output: Contribution to journalArticle

Lan, K, McAferty, K, Shah, P, Lieberman, E, Patel, DR, Cook, CB & LaBelle, J 2011, 'A disposable tear glucose biosensor - Part 3: Assessment of enzymatic specificity', Journal of diabetes science and technology, vol. 5, no. 5, pp. 1108-1115. https://doi.org/10.1177/193229681100500511
Lan, Kenneth ; McAferty, Kenyon ; Shah, Pankti ; Lieberman, Erica ; Patel, Dharmendra R. ; Cook, Curtiss B. ; LaBelle, Jeffrey. / A disposable tear glucose biosensor - Part 3 : Assessment of enzymatic specificity. In: Journal of diabetes science and technology. 2011 ; Vol. 5, No. 5. pp. 1108-1115.
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abstract = "Background: A concept for a tear glucose sensor based on amperometric measurement of enzymatic oxidation of glucose was previously presented, using glucose dehydrogenase flavin adenine dinucleotide (GDH-FAD) as the enzyme. Glucose dehydrogenase flavin adenine dinucleotide is further characterized in this article and evaluated for suitability in glucose-sensing applications in purified tear-like saline, with specific attention to the efect of interfering substances only. These interferents are specifically saccharides that could interact with the enzymatic activity seen in the sensor's performance. Methods: Bench top amperometric glucose assays were performed using an assay solution of GDH-FAD and ferricyanide redox mediator with samples of glucose, mannose, lactose, maltose, galactose, fructose, sucrose, and xylose at varying concentrations to evaluate specificity, linear dynamic range, signal size, and signal-to-noise ratio. A comparison study was done by substituting an equivalent activity unit concentration of glucose oxidase (GOx) for GDH-FAD. Results: Glucose dehydrogenase flavin adenine dinucleotide was found to be more sensitive than GOx, producing larger oxidation currents than GOx on an identical glucose concentration gradient, and GDH-FAD exhibited larger slope response (-5.65 × 10-7 versus -3.11 × 10-7 A/mM), signal-to-noise ratio (18.04 versus 2.62), and linear dynamic range (0-30 versus 0-10 mM), and lower background signal (-7.12 versus -261.63 nA) than GOx under the same assay conditions. GDH-FAD responds equally to glucose and xylose but is otherwise specific for glucose. Conclusion: Glucose dehydrogenase flavin adenine dinucleotide compares favorably with GOx in many sensor-relevant attributes and may enable measurement of glucose concentrations both higher and lower than those measurable by GOx. GDH-FAD is a viable enzyme to use in the proposed amperometric tear glucose sensor system and perhaps also in detecting extreme hypoglycemia or hyperglycemia in blood.",
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AB - Background: A concept for a tear glucose sensor based on amperometric measurement of enzymatic oxidation of glucose was previously presented, using glucose dehydrogenase flavin adenine dinucleotide (GDH-FAD) as the enzyme. Glucose dehydrogenase flavin adenine dinucleotide is further characterized in this article and evaluated for suitability in glucose-sensing applications in purified tear-like saline, with specific attention to the efect of interfering substances only. These interferents are specifically saccharides that could interact with the enzymatic activity seen in the sensor's performance. Methods: Bench top amperometric glucose assays were performed using an assay solution of GDH-FAD and ferricyanide redox mediator with samples of glucose, mannose, lactose, maltose, galactose, fructose, sucrose, and xylose at varying concentrations to evaluate specificity, linear dynamic range, signal size, and signal-to-noise ratio. A comparison study was done by substituting an equivalent activity unit concentration of glucose oxidase (GOx) for GDH-FAD. Results: Glucose dehydrogenase flavin adenine dinucleotide was found to be more sensitive than GOx, producing larger oxidation currents than GOx on an identical glucose concentration gradient, and GDH-FAD exhibited larger slope response (-5.65 × 10-7 versus -3.11 × 10-7 A/mM), signal-to-noise ratio (18.04 versus 2.62), and linear dynamic range (0-30 versus 0-10 mM), and lower background signal (-7.12 versus -261.63 nA) than GOx under the same assay conditions. GDH-FAD responds equally to glucose and xylose but is otherwise specific for glucose. Conclusion: Glucose dehydrogenase flavin adenine dinucleotide compares favorably with GOx in many sensor-relevant attributes and may enable measurement of glucose concentrations both higher and lower than those measurable by GOx. GDH-FAD is a viable enzyme to use in the proposed amperometric tear glucose sensor system and perhaps also in detecting extreme hypoglycemia or hyperglycemia in blood.

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