Glucose Determination by Means of Steady-state and Time-course UV Fluorescence in Free or Immobilized Glucose Oxidase

Luca, Paola De; Lepore, Maria; Portaccio, Marianna; Esposito, Rosario; Rossi, Sergio; Bencivenga, U.; Mita, Damiano Gustavo

doi:10.3390/s7112612

Cited by 17 publications

(11 citation statements)

References 24 publications

(35 reference statements)

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“…Dynamical changes of FAD fluorescence are exhibited when oxidative processes are induced in GOD by means of glucose interaction [21–23]. In fact, GOD catalyses the oxidation of glucose to gluconic acid through the reaction:

\begin{array}{l} left & D - glucose + 0_{2} \overset{italicGOD}{true\to} D - gluconolactone + H_{2} 0_{2} \\ left & D - gluconolactone + H_{2} 0 \to D - gluconic acid \end{array}

The well-known reaction mechanism is the following: glucose reduces FAD to FADH 2 with formation of gluconolactone, which is rapidly hydrolysed to gluconic acid.…”

Section: Introductionmentioning

confidence: 99%

Glucose Sensing by Time-Resolved Fluorescence of Sol-Gel Immobilized Glucose Oxidase

Esposito

Ventura²,

Nicola

et al. 2011

Sensors

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A monolithic silica gel matrix with entrapped glucose oxidase (GOD) was constructed as a bioactive element in an optical biosensor for glucose determination. Intrinsic fluorescence of free and immobilised GOD was investigated in the visible range in presence of different glucose concentrations by time-resolved spectroscopy with time-correlated single-photon counting detector. A three-exponential model was used for analysing the fluorescence transients. Fractional intensities and mean lifetime were shown to be sensitive to the enzymatic reaction and were used for obtaining calibration curve for glucose concentration determination. The sensing system proposed achieved high resolution (up to 0.17 mM) glucose determination with a detection range from 0.4 mM to 5 mM.

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\begin{array}{l} left & D - glucose + 0_{2} \overset{italicGOD}{true\to} D - gluconolactone + H_{2} 0_{2} \\ left & D - gluconolactone + H_{2} 0 \to D - gluconic acid \end{array}

The well-known reaction mechanism is the following: glucose reduces FAD to FADH 2 with formation of gluconolactone, which is rapidly hydrolysed to gluconic acid.…”

Section: Introductionmentioning

confidence: 99%

Glucose Sensing by Time-Resolved Fluorescence of Sol-Gel Immobilized Glucose Oxidase

Esposito

Ventura²,

Nicola

et al. 2011

Sensors

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“…This model has recently been used by other a b Fig. 4 authors [67]. For low glucose concentration this expression can be simplified to [68]:…”

Section: Sensors Based On Gox Fluorescencementioning

confidence: 97%

“…This makes the method very prone to interference and greatly complicates sensor device development because most of the solid matrix absorbs in this zone. Despite these problems, this methodology has been recently implemented in gelatine sensors [67].…”

Section: Sensors Based On Gox Fluorescencementioning

confidence: 99%

Reagentless fluorescent biosensors based on proteins for continuous monitoring systems

et al. 2012

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There is a lack of commercially available efficient and autonomous systems capable of continuous monitoring of (bio)chemical data for clinical, environmental, food, or industrial samples. The weakest link in the design of these systems is the (bio)chemical receptor (bCR). The bCR should have transducer ability, the recognition event should be a single reaction, and the bCR should be easily regenerated. Transport proteins and enzymes are well placed as bCR for optical continuous monitoring systems (OCMS). In this paper we review quantitative aspects and the main transducer strategies which have been developed for transport proteins, using periplasmic binding proteins (linking an environmentally sensitive fluorophore or FRET between two fluorophores) and concanavalin A (competitive reversible assays) as representative examples. Efficient immobilization systems and implementation in OCMS are also reviewed. Some kinds of enzymes can fulfil the necessary requirements to be appropriate bCR. Strategies using flavoenzymes chemically modified with fluorophores can be successfully implemented in OCMS and they are, in our opinion, the most appropriate option.

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“…Recent years have witnessed remarkable progress in the design of glucose measurement based on enzymatic assay due to its high specificity, reliability, and simplicity compared to other chemical methods . Among them, the glucose oxidase (GOx)/horseradish peroxidase (HRP) (GOP) is a coupled enzymatic assay commonly used in measuring glucose concentrations in biological sciences and food chemistry, particularly for quantification of α‐glucosidase activity and screening its inhibition .…”

Section: Introductionmentioning

confidence: 99%

Ultrasensitive analysis of glucose in serum by capillary electrophoresis with LIF detection in combination with signal amplification strategies and on‐column enzymatic assay

Guan

Zhou

2016

Electrophoresis

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A highly specific and sensitive method for glucose quantification in human serum samples based on on-column enzymatic assay is described. In this method, the head of the capillary was used as a nanoliter-microreactor, the diluted samples spiked with a novel fluorogenic reagent named 2-[6-(4'-amino) phenoxy-3H-xanthen-3-on-9-yl] benzoic acid (APF), and the mixed enzyme solutions of glucose oxidase (GOx) and horseradish peroxidase (HRP), were individually injected into the capillary. Hydrogen peroxide (H2 O2 ) generated in situ by catalytic reaction between GOx and glucose, activates APF in the presence of HRP to form a highly fluorescent product, which was electrophoretically separated from the unreacted APF and detected by the LIF detector. The proposed method allowed the determination of glucose down to 10 nM in real samples, with RSD values lower than 3.5%, which also has the potential for measurements of multicomponents in many other systems including measurement of α-glucosidase activity and screening for its inhibitors.

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Glucose Determination by Means of Steady-state and Time-course UV Fluorescence in Free or Immobilized Glucose Oxidase

Cited by 17 publications

References 24 publications

Glucose Sensing by Time-Resolved Fluorescence of Sol-Gel Immobilized Glucose Oxidase

Glucose Sensing by Time-Resolved Fluorescence of Sol-Gel Immobilized Glucose Oxidase

Reagentless fluorescent biosensors based on proteins for continuous monitoring systems

Ultrasensitive analysis of glucose in serum by capillary electrophoresis with LIF detection in combination with signal amplification strategies and on‐column enzymatic assay

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