Recent developments and applications of chemiluminescence sensors

Analytica Chimica Acta 541 (2005) 37–47

Review

Recent developments and applications of chemiluminescence sensors Zhenyu Zhang, Sichun Zhang, Xinrong Zhang ∗ Department of Chemistry, Key Laboratory for Atomic and Molecular Nanosciences of Education Ministry, Tsinghua University, 100084 Beijing, PR China Received 1 July 2004; received in revised form 29 November 2004; accepted 29 November 2004 Available online 2 February 2005

Abstract This is a brief review on the developments and applications of chemiluminescence (CL) sensors dated from 1999 to present. Methods and materials for immobilization of CL reagents are introduced. The CL-based sensors, including the sensors for the detection of inorganic species, organic species and biological macromolecules are summarized. The advantages and limitations of CL sensors are discussed. © 2004 Elsevier B.V. All rights reserved. Keywords: Chemiluminescence sensor; Immobilized reagents; Inorganic and organic species; Nucleic acid; Drug; Antibody; Protein

Contents 1. 2.

3.

Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Progress in methodology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2.1. Immobilization of CL reagents on ion-exchange resins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2.2. Immobilization of enzymes on polymer or in sol–gel . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2.3. Immobilization on other materials . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Analytical applications . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.1. CL sensors for inorganic compounds . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.1.1. H2 O2 sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.1.2. Ammonium CL sensor . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.1.3. Phosphate CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.1.4. Sulfite CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.1.5. O3 gas CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.1.6. N-containing gas CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.1.7. Cl2 CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2. CL sensors for organic and biological compounds . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.1. Amino acids CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.2. Vitamin CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.3. Cholesterol CL sensor . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.4. Adrenaline and isoprenaline CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.5. Acetylcholine and choline CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.6. Urea and uric acid CL sensors. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.7. Glucose CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .

∗

Corresponding author. Tel.: +86 10 6278 7678; fax: +86 10 6277 0327. E-mail addresses: [email protected] (Z. Zhang), [email protected] (X. Zhang). 0003-2670/$ – see front matter © 2004 Elsevier B.V. All rights reserved. doi:10.1016/j.aca.2004.11.069

38 38 38 39 39 39 39 39 39 40 40 40 40 40 40 40 41 41 42 42 42 42

38

4.

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

3.2.8. Glycolic acid CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.9. Nucleic acid CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.2.10. Protein CL sensors. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3. CL sensors for drug analysis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3.1. Analgin CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3.2. Antibiotics CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3.3. Dopamine CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3.4. Isoniazid CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3.5. Ofloxacin CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3.6. Pipemidic acid CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3.7. Reserpine, novalgin and berberine CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3.3.8. Pesticide or herbicide CL sensors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Conclusions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Acknowledgement . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .

1. Introduction Chemical sensor is nowadays one of the most active research fields due to their high sensitivity and selectivity with small size for portable applications. According to the origin of the obtainable signals, these sensors can be roughly classified into electrochemical sensors and optical sensors, the latter mainly utilizing the principles of absorbance, photoluminescence and chemiluminescence (CL) detection. In recent years, there has been a great deal of interests in the development of CL-based sensors due to their high sensitivity compared with photoluminescence-based sensors. This promoted sensitivity of CL-based sensing system is ascribed to the avoidance of the noise caused by light scattering, and features simpler set-up with lower background emissions in comparison with photoluminescence detection. However, one of the major deficiencies in applying CL sensors to routine analysis was the short lifetime and signal drift due to the irreversible consumption of CL reagents that have limited the application of CL sensors in practice. Although several CL sensors have been designed on the basis of recycled usage of CL reagents bound to polymers, that decreased the consumption of the luminescent reagent during detection, the stability of this type of sensors is still compromised because of the reagents bleaches or partitions into hydrophobic regions of the film over time. Up to now, it is still a challenge to develop CL sensors that are not only sensitive enough, but also stable and simple with long lifetime for practical applications. In the present paper, recent developments and applications of CL sensors are reviewed. The literature dates from 1999 to present. The literature before 1999 has been extensively reviewed in earlier publications [1–3].

2. Progress in methodology The selectivity, sensitivity and lifetime of the CL sensors would be greatly dependent on the following points: (1) the

42 42 43 43 43 43 43 43 43 43 43 43 45 46 46

careful selection of CL reagents responding to the definite species, (2) the way to immobilize the reagents, and (3) the substrates selected for reagents immobilization. Reagents immobilization onto proper substrates plays an important role in the development of the high-quality CL-based sensors. 2.1. Immobilization of CL reagents on ion-exchange resins Since most of the established CL systems are operated in aqueous solutions and the CL reagents are various ions, ion exchange resins have been selected as one of the most popular substrates for reagents immobilization. Due to the high surface coverage and convenient immobilization procedure for CL reagents, the ion-exchange approach has been widely used to immobilize CL reagents to develop a series of CL sensors. By injection of appropriate eluents the immobilized reagents could be released quantitatively from the ion-exchange column to perform CL reaction. The analytes can also react directly with the immobilized reagents, thus permitting the sensors to operate in a reagentless way. The immobilization of luminol and other CL reagents on ion-exchange resins have been extensively employed to develop various CL sensors. Generally, the resins with immobilized CL reagents were mixed and packed into a piece of glass tube, which served as a flow cell and was positioned in front of the detection window of a photomultiplier. Zhang and co-workers [4–10] proposed a type of so-called bleeding CL sensors for the determination of inorganic and some organic analytes. The sensors were prepared by electrostatically immobilizing CL reagents and some metal ions [5], such as Co(II), Cu(II), or Fe(CN)6 3− on anion/cation exchange columns. The analytes, such as H2 O2 , could be detected based on the CL reaction of luminol and metal ions bleeding from the ion exchange columns. Problems with this arrangement included unnecessary dilution of the eluted reagents and samples, which reduced the detectability. Also, the need to merge two streams prior to detection made it difficult to miniaturize the configuration.

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

The consumption of reagents that accompanies CL reactions resulted in the deterioration of the sensors on prolonged use. A promising way to solve this problem was to immobilize CL regents that can recycle. Lin et al. [11] have developed a CL sensor by immobilizing tris-(2,2 -bipyridyl)ruthenium(II) complex (Ru(bpy)3 2+ ) on the Dowex-50 W cationic ionexchange resin. They found that the Ru(bpy)3 2+ immobilized resin could be used at least for 6 months. 2.2. Immobilization of enzymes on polymer or in sol–gel The immobilization of enzymes is one of the popular routes to develop chemical and biological sensors, because enzyme acts as high active and high selective catalyst. Highly sensitive and selective CL sensors can be obtained without the consumption of enzyme. Although enzyme-loaded polymer membranes have been widely used to prepare CL sensors, the limited operational stability of the enzyme sensors is the main hindrance to their wider application to solve analytical problems. The use of sol–gel to immobilize enzymes has become a recognized process for preparing CL sensor. The key advantages of sol–gel are that there is little or no structural alteration of the encapsulate species and it is suitable for optical sensors due to its optical transparency and chemical stability. It has been reported that horseradish peroxidase (HRP) encapsulated in a sol–gel substrates exhibited excellent characteristics in terms of activity, lifetime and optical transparency [12]. This advantage has been further demonstrated by the sol–gel immobilized hemoglobin as catalyst as well [13]. Although it is not synthesized artificially, natural plant and animal tissues offers superior biocompatibility to the enzymes, leading to the high activity and long lifetime of the enzymes. Therefore plant and animal tissues have been used to construct CL sensors with the advantages of low cost, high activity and stability, as well as longer lifetime. These advantages have been demonstrated by several CL sensors such as the soybean tissue-based CL biosensor for urea [14] and spinach tissue-based CL biosensor for glycolic acid [15], etc. 2.3. Immobilization on other materials To improve the performance of CL sensors, much attention has been paid to employing new materials as substrates for CL reagent immobilizations. Molecular imprinting technique is a rapidly developing technique for the preparation of polymers that would be used as sensing materials to design CL sensors. The imprinted cavities of a defined shape and functional groups in the molecularly imprinted polymer are expected to develop not only with the molecule recognition function but also as a special CL reaction medium. Two CL sensors [16,17] based on molecular imprinting technique have shown the potential for sensing dansyl-l-phenylalanine and 1,10-phenanthroline. The expanding availability of nanoparticles has attracted widespread attention in catalysis due to their high surface

39

areas, high activity and good selectivity. Several types of nanosized materials have been investigated in our laboratory [18–22]. The CL has been detected on the nanosized materials while organic molecules are passing through their surface. In comparison with conventional CL sensors, the sensors based on nanosized materials offer advantages that there is no consumption of CL reagents, and the size of the sensors can be miniaturized due to the small size of nanoparticles. All sensors exhibit good stability and durability. The immobilization procedure sometimes can be omitted by simply fixing the slight-soluble metal oxides particles onto membranes or in columns. This type of CL sensors offers advantages of simple preparation and long lifetime. For example, the solid-phase manganese dioxide particles have been fixed on the sponge rubber inside the CL flow cell for the detection of analgin [23]. The solid-phase PbO2 [24] and sodium bismuthate [25] were also fixed inside of the CL flow cells for the determinations of ofloxacin and pipemidic acid, respectively.

3. Analytical applications 3.1. CL sensors for inorganic compounds 3.1.1. H2 O2 sensors Although CL sensors for H2 O2 have been extensively studied in the past decade, they still attracted much attention because of the importance of H2 O2 in bioanalysis as an indicator for enzyme detection. Several H2 O2 CL sensors have been designed based on the traditional CL reaction between H2 O2 and luminol, catalytized by enzymes, such as HRP [12,26–28], or hemoglobin [13]. This type of CL sensors offers high sensitivity as reported by most publications. For example, the detection limit of 4.0 × 10−8 M was obtained with immobilized HRP as catalyst [26]. By using hemoglobin as catalyst, a detection limit of 1.3 × 10−7 M was also reported [13]. Qu et al. [29] have developed a CL sensor for H2 O2 based on immobilization of plant tissues containing enzymes. Apart from immobilization of enzyme and issues, Lin and coworkers [30,31] have developed a CL sensor for H2 O2 by using a heterogeneous catalyst, Co(II)-ethanolamine complex with the detection limit of 1 × 10−7 M. In addition, Kiba et al. [32] have developed a micromachined flow cell (overall size 25 mm × 25 mm × 1 mm) for the fast determination of H2 O2 , based on a luminol–H2 O2 CL reaction catalyzed by peroxidase. Marquette and Blum [33] have developed a biochip based on the immobilization of glucose oxidase (GOx) to detect H2 O2 . The different light intensities measured simultaneously on the entire array with a CCD camera. The H2 O2 concentration down to 5 nM could be detected. 3.1.2. Ammonium CL sensor A CL sensor for the detection of NH4 + ions was developed by Qin et al. [34] based on the inhibition effect of NH4 + ions on the CL reaction between luminol and chlorine. Trace NH4 +

40

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

ions (down to 0.4 ␮M) could be detected with this CL sensor. The chlorine was online generated electrochemically from hydrochloric acid in a coulometric cell. The system remained stable for over 500 determinations. 3.1.3. Phosphate CL sensors An automated flow-injection sensor by combining a pyruvate oxidase reaction and CL reaction for the detection of phosphate ion in river water has been developed by Nakamura et al. [35]. The detection limit was 96 nM phosphate ions. This sensor was sufficient to determine the maximal permissible phosphate-ion concentration in the environmental waters of Japan. The same authors also examined the possibilities for the construction of sensors using the combinations of several enzymes without the need for coenzymes, and developed a phosphate ion biosensor based on a maltose phosphorylase, mutarotase, and glucose–oxidase (MP–MUT–GOD) reaction combined with an arthromyces ramosus peroxidase–luminol reaction system. The response provided by this system was linear, with a wide range between 10 and 30 nM phosphate ion [36,37]. Morais et al. [38] described a CL sensor for the trace determination of orthophosphate in waters. The proposed sensor relies upon the in-line derivatisation of the analyte with ammonium molybdate in the presence of vanadate, and the transient immobilization of the resulting heteropolyacid in a copolymer packed spiral shape flow-through cell. This sensor avoided drawbacks of the excess of molybdate anion, which causes high background signals due to its selfreduction and accommodate reactions with different pH requirements and the ability to determine trace levels of orthophosphate in high silicate content samples. 3.1.4. Sulfite CL sensors Based on the CL produced by auto-oxidation of sulfite in the presence of Rh6G, a sulfite sensor was developed by Huang et al. [39]. The system responded linearly to sulfite concentration in the range of 0.01–5 mg l−1 with a detection limit of 0.01 mg l−1 . Lin et al. [11] have developed a flowthrough CL sensor to determine sulfite based on Ru(bpy)3 2+ reagent. The limit of detection was 1 × 10−7 M. 3.1.5. O3 gas CL sensors Although a majority of the researchers have focused their attention on the development of CL liquid sensors, there were still a few reports concerning the CL gas sensors in recent years. Takayanagi et al. [40] have reported an O3 sensor based on interfacial gas–liquid CL on a wetted transparent screen directly on top of a miniature photomultiplier tube. Alkaline chromotropic acid (CA) gives out photons upon exposure to ozone. Another O3 CL sensor was described by Eipel et al. [41]. This sensor was characterized by a continuously renewing of the CL reagent as a thin film on a smooth glass surface with a very small liquid flow rate, which resulted in decreased consumption of reagents. Yushkov et al. [42] reported a commercial CL sensor for O3 detection at altitude of about 20,000 m and a temperature of about −75 ◦ C. A com-

parison between the results was obtained during a test flight with those derived from a contemporary balloon sounding. Another commercial O3 CL sensor [43] was developed for the observation of atmospheric trace gases and aerosols in the tropopause region, which allows a systematic collection of relevant data at comparatively low costs. 3.1.6. N-containing gas CL sensors A gas CL sensor for NO has been developed by Evmiridis and co-workers [44] for the monitoring of NO in biological fluids. The composite cellulose acetate film coated with Nafion was utilized to achieve a sufficient diffusion rate of NO and high selectivity towards various interfering compounds present in blood. HRP was used as NO trapper to form stable compound HRP–NO. The NO concentration down to 0.9 × 10−6 mol could be detected [44]. By miniaturizing the sensor into a microprobe based on microdialysis techniques, the same authors developed a sensor that was sensitive enough to detect variations of NO formation under different physiological states in vivo. The real NO concentrations in test animals used in reported work were found to be in the range of 1–5 nM or even less [45]. A NH3 CL sensor was demonstrated by Shi et al. [46] by the combination of a nanosized NH3 converter with CL detector. The NH3 gas was firstly oxidized on nanosized LaCoO3 to produce NOx , which could react with luminol to generate CL emission. The method allows detecting NH3 down to 0.014 ppm. The CL sensor [47] for hydrazine detection was described by using luminol and hexacyanoferrate(III) that were immobilized on an anion-exchange column. The CL emission from the reaction was decreased in the presence of hydrazine above 0.04 ng ml−1 . 3.1.7. Cl2 CL sensors Nakamura et al. [48] have explored the CL reaction of bis(2,4,6-(trichlorophenyl)-oxalate) (TCPO) with free chlorine as oxidant in the presence of fluorophore and developed an analytical method by FIA for free chlorine determination in tap water. Eight fluorophores were tested and 9,10diphenylanthracene showed the best sensitivity and solubility. The detection limit was 2.0 × 10−6 M for free chloride. Table 1 gives the summary of CL sensors developed for inorganic compounds. 3.2. CL sensors for organic and biological compounds 3.2.1. Amino acids CL sensors CL sensors for the determination of amino acids were essentially based on enzyme reactions. The CL biosensor for the determination of total d-amino acid has been reported by the immobilization of d-amino acid oxidase onto aminemodified silica gel via glutaraldehyde activation. The H2 O2 produced from the enzyme column was reacted with luminol and ferricyanide [49]. The detection limit was 4.5 × 10−7 M d-amino acid. Another CL enzymatic sensor [50] was developed for the determination of l-aspartate in a medium

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

41

Table 1 CL sensors for inorganic compounds Analyte Chlorine ClO− CCl4 H 2 O2 H2 O2 H2 O2 H2 O2 H2 O2 H2 O 2 H2 O 2 H2 O 2 H2 O2 H2 O2 Hydrazine NH3 NO NO NO O3 O3 Orthophosphate PO4 3− PO4 3− Sulfite Sulfite

CL reaction system

Linear range

Detection limit

Reference

Chlorine–bis(2,4,6-(trichlorophenyl)-oxalate)-9,10diphenylanthracene Hydrogen peroxide–indole–ClO− O2 –CCl4 –TiO2 –luminol H2 O2 –luminol–HRP H2 O2 –luminol–HRP H2 O2 –luminol–hemoglobin H2 O2 –luminol–HRP H2 O2 –luminol–HRP H2 O2 –luminol–HRP H2 O2 –luminol–glucose oxidase H2 O2 –luminol–potato tissue HRP H2 O2 –luminol–Co(II)–ethanolamine complex Hydrazine–luminol–hexacyanoferrate(III) O2 –NH3 –LaCoO3 –luminol O2 –NO–chromium trioxide–luminol H2 O2 –luminol–HRP–NO compound H2 O2 –luminol–HRP–NO compound O3 –alkaline chromotropic acid O3 –azine dyes ammonium molybdate–vanadate–orthophosphate–luminol

(0.2–3.0) × 10−5

2.0 × 10−6

M

[48]

5 ng ml−1 40 ppb 8 × 10−3 mM 2.8 × 10−7 M 1.3 × 10−7 M 4.0 × 10−8 M

2 × 10−7 to 2 × 10−5 M 0.1–100.0 ng ml−1 0.04–10 ppm 1–100 ppbv 1.8 × 10−6 to 2.7 × 10−3 mol 5 nM to 1 ␮M Up to 230 ppbv 5.2–330 ␮g m−3

0.6 pmol 5 nM 4 × 10−7 M 15 pmol 1 × 10−7 M 0.04 ng ml−1 0.014 ppm 0.3 ppbv 0.9 × 10−6 mol 1 nM 40 pptv 2.1 ␮g m−3

[81] [82] [12] [83] [13] [26] [27] [28] [33] [29] [58] [30] [47] [46] [84] [44] [45] [40] [41]

5–50 ␮g l−1 96 nM to 32 mM

4 ␮g l−1 96 nM

[38] [35]

0.01–5 mg l−1

0.1–30 ␮M 0.01 mg l−1 1 × 10−7 M

[36] [39] [11]

O2 –Pyruvate–phosphate–pyruvate oxidase–G-luminol MP–MUT–GOD–luminol–peroxidase O2 –sulfite–R6G Ru(bpy)3 2+ –KMnO4 or Ce(SO4 )2

M

5–500 ng ml−1 0.1–380 ppm Up to 2 mM 1 × 10−4 to 8 × 10−7 M 6 × 10−5 to 4 × 10−7 M 1.0 × 10−7 to 1.0 × 10−5 M 4 and 1000 ␮M 0.61–9.7 ␮M 5 nM to 1mM 1.0 × 10−6 to 1.0 × 10−3 M

HRP: horseradish peroxidase.

for mammalian cell cultivation based on the immobilization of aspartate, aminotransferase and l-glutamate oxidase on sieved porous glass beads. At first, l-aspartate is converted to oxalacetate generating l-glutamate catalyzed by aspartate aminotransferase. Then l-glutamate oxidase catalyzes the oxidation of l-glutamate and generate H2 O2 , which was detected by luminol CL reaction. A CL flow sensor [51] for the determination of l-glutamate in serum was developed by using oxidases such as glutamate oxidase (GOD), uricase (UC) and peroxidase (POD). l-Glutamate in the sample plug was enzymatically converted to H2 O2 with immobilized GOD. Subsequently, the peroxide reacts with luminol on the immobilized POD to produce CL. The detection limit was 10 nM. Janasek and Spohn [52] developed a CL sensor for the determination of l-alanine, alpha-ketoglutarate and lglutamate in the cultivation medium of mammalian cells by using a microreactor containing alanine aminotransferase and glutamate oxidase immobilized on sieved porous glass beads for the generated H2 O2 . To catalyze the indicator reaction between luminol and H2 O2 , both Co2+ and immobilized peroxidase were used in a fiber optic detector cell. l-Alanine, alpha-ketoglutarate and l-glutamate can be detected with detection limits of 2, 5 and 1 nM, respectively. Lin and Yamada [16] have developed a CL sensor based on molecular imprinting recognition. As an initial attempt, dansyl-l-phenylalanine (dns-l-Phe) was used as a template

molecule and methacrylic acid and 2-vinylpyridine were used as functional monomers. When the flowing streams of KHSO5 and Co2+ solutions mixing through the molecularly imprinted polymer particles filled the flow cell, the template molecule, dansyl-l-phenylalanine, reacted with the KHSO5 /Co2+ solution and CL was emitted. 3.2.2. Vitamin CL sensors A CL sensor for Vitamin K-3 (menadione sodium bisulfite, MSB) has been developed based on the auto-oxidation of bisulfite liberated from MSB in alkaline media in the presence of Tween 80 sensitized by Rh6G immobilized on a cationexchange column. The sensor responds linearly to the MSB concentration in the range of 0.5–10 ng ml−1 with a detection limit of 2.6 ng l−1 [53]. Based on the enhance effect of riboflavin on the luminol–periodate CL reaction, a flow CL riboflavin sensor [54] was developed. The increase of CL emission was correlated with the riboflavin concentration in the range from 0.04 to 200 ng ml−1 . 3.2.3. Cholesterol CL sensor Immobilizing cholesterol oxidase onto amine-modified silica gel via glutaraldehyde activation and packed in a column, a CL biosensor has been developed for determining cholesterol. The analytical reagents, including luminol and ferricyanide, were electrostatically coimmobilized on an

42

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

anion-exchange column. Cholesterol was detected by the CL reaction between H2 O2 released from the enzymatic reaction with luminol and ferricyanide. The detection limit of the sensor was 5 × 10−6 g ml−1 cholesterol [55]. 3.2.4. Adrenaline and isoprenaline CL sensors It was found that adrenaline and isoprenaline could greatly enhance the CL emission between luminol and periodate in alkaline solution. Based on the fact, a CL flow sensor [56] has been developed for adrenaline and isoprenaline determination. The sensor allowed the determination of adrenaline and isoprenaline over the range from 2.0 × 10−8 to 1.0 × 10−5 and from 2.0 × 10−7 to 5.0 × 10−5 g ml−1 , respectively. 3.2.5. Acetylcholine and choline CL sensors A CL sensor with good selectivity and stability for detection of acetylcholine (Ach) and choline (Ch) has been reported [57]. The activated dialysis tubing has been used as a support film, and the related enzymes were immobilized on the surface of activated dialysis tubing with the help of polyacrylamide gel based on the biotin–streptavidin system. The H2 O2 that was generated in enzymatic conversion action from Ach or Ch was detected through the luminol–hexacyanoferrate CL reaction. The Ch concentration down to 0.03 pmol and the Ach concentration down to 1.2 pmol could be detected. Another Ch biosensor [58] was developed based on a sensing layer by the non-covalent immobilization of enzymes on derivatized Sepharose beads subsequently entrapped in a photopolymer. The limit of detection for choline down to 0.5 pmol was obtained with this sensor. The sensor for the simultaneous determination of Ch and Ach [59] was also developed based on a sensitive trienzyme CL biosensor. Two-peak response was obtained by one injection of the sample solution. The first and second peaks were dependent on the concentrations of Ch and ACh, respectively. Calibration curves were linear at 1–1000 nM for Ch and 3–3000 nM for ACh. 3.2.6. Urea and uric acid CL sensors A plant tissue-based CL biosensor for urea was reported by packing soybean tissue in a mini-glass column [14]. The urease-catalyzed reaction occurred in the plant tissue column to produce NH4 + and HCO3 − . The anion produced could release luminol from the anion-exchange column with immobilized luminol, which then reacted with permanganate eluted from the anion-exchange permaganate column with sodium hydroxide, thus producing a CL signal. The CL intensity was linear with urea concentration in the range 4–400 mM. The uric acid could also be detected based on the enzymatic reaction to produce H2 O2 , catalyzed by uricase [60]. A microprobe was modified and coated with immobilized enzyme through a Streptavidin–biotin mediated linker by using a chitosan support membrane, and polyurethane trapped ferrocene film was employed to protect the probe surface and diminish the interference from reductant molecules, which are often present in the blood (e.g. ascorbic acid). The constructed

sensor could detect uric acid in the range of 0.01–1 mM with detection limit of 5 ␮M. Based on the inhibition effect of uric acid on the CL produced by the reaction between luminol and periodate, a CL uric acid sensor has been developed with the detection limit of 1.8 ng ml−1 [61]. 3.2.7. Glucose CL sensors A CL biosensor on a chip coupled to microfluidic system [62] was developed by immobilizing GOD onto controlledpore glass via glutaraldehyde activation. The glucose was detected based on the CL reaction between H2 O2 produced from the enzymatic reaction and CL reagents, which were released from the anion-exchange resin. Based on similar method described for H2 O2 detection, a heterogeneous CL glucose sensor was developed by Lin et al. [30]. The CL intensity versus glucose concentration was linear within the range 1.0 × 10−6 to 1 × 10−4 M. Marquette and Blum [33] have developed a CL sensor that exhibited good performances with a detection limit of 7.5 nM glucose. 3.2.8. Glycolic acid CL sensors A plant tissue-based CL biosensor [15] for glycolic acid was developed by immobilizing the spinach tissue in a glass column. Glycolic acid was oxidized by oxygen under the catalysis of glycolate oxidase to produce H2 O2 , which could react with luminol in the presence of peroxidase of spinach tissue to generate CL signals. This biosensor was reported to be stable for about 3 weeks. 3.2.9. Nucleic acid CL sensors Xu et al. [63] reported a CL biosensing method in which the captured probe was immobilized on a gold surface by the self-assembly technique. The complementary sequence was detected by coupling avidin–alkaline phosphatase to the biotinylated oligonuclotide and measuring the CL signal obtained from the hydrolysis of the substrate 3-(2 spiroadamantane)-4-methoxy-4-(3 -phosphoryloxy) phenyl1,2-dioxetane (AMPPD) by this enzyme. Another CL biosensor for nucleic acid was described by Jiang et al. [64]. Gold surface was modified with N-acetylcysteine to produce a self-assembled monolayer. A single layer film of biotinylated oligonucleotide probes was constructed by binding to a precursor layer of streptavidin which had been immobilized on modified gold surface covalently using carbodiimide hydrochloride (EDC) and N-hydroxysuccinimide (NHS). A sandwich solution hybridization was executed with immobilized DNA, target DNA and second biotinylated DNA probes. Then extravidin alkaline phosphatase, which can dephosphorylate AMPPD substrates to produce stable intermediates that produce a measurable yield of light output was bound with second hybridized biotinylated DNA probes. Hepatitis B virus (HBV) DNA fragment was measured with a detection limit of 3 × 10−14 M HBV DNA. A CL DNA biosensor [65] based on fiber-optic was also developed. DNA probes were covalently immobilized onto the distal end of the optical

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

fiber bundle. Hybridization of HRP-labeled complementary nucleotides to the immobilized probes was detected by enhanced CL. 3.2.10. Protein CL sensors An immunosensor involving use of the fiber optics in combination with CL has been developed by Starodub et al. [66] for monitoring biological pollutants (yeast cells and their components) discharged into the air from a biotechnological plant producing lysine. The HRP labeled antibody was applied for immunoreaction. The CL emission was generated by the enhanced CL in the oxidation of luminol by H 2 O2 . 3.3. CL sensors for drug analysis 3.3.1. Analgin CL sensors A CL analgin sensor [23] has been developed based on the oxidation of analgin by manganese dioxide to produce a weak CL. The CL intensity was enhanced by the addition of rhodamine B. The calibration graph was linear in the range from 4 × 10−5 to 1 × 10−3 g ml−1 and could be used continuously 400 times. Another CL flowthrough sensor [67] for the determination of analgin was developed based on the auto-oxidation of analgin by O2 in the presence of Tween 80 sensitized by Rh6G immobilized on a cation-exchange column. Based on the inhibition effect of analgin on the CL signals produced by the reaction between luminol and periodate, Song and Zhang [68] reported a sensitive CL analgin sensor that could be used for the determination of analgin with a detection limit of 0.04 ng ml−1 . 3.3.2. Antibiotics CL sensors A parallel affinity sensor array (PASA) for the rapid automated analysis of 10 antibiotics in milk is presented by Knecht et al. [69], using multianalyte immunoassays with an indirect competitive ELISA format. Microscope glass slides modified with (3-glycidyloxypropyl) trimethoxysilane were used for the preparation of hapten microarrays. Protein conjugates of the haptens were immobilized as spots on disposable chips, which were processed in a flow cell. Monoclonal antibodies against penicillin G, cloxacillin, cephapirin, sulfadiazine, sulfamethazine, streptomycin, gentamicin, neomycin, erythromycin, and tylosin allowed the simultaneous detection of the respective analytes. Antibody binding was detected by a second antibody labeled with horseradish peroxidase generating enhanced CL, which was recorded with a sensitive CCD camera. The detection limits ranged from 0.12 to 32 ␮g l−1 . 3.3.3. Dopamine CL sensors A plant tissues-based CL biosensor [70] has been fabricated for dopamine determination. Dopamine is oxidized under the catalysis of polyphenol oxidase in the tissue column to produce hydrogen peroxide, which can react with

43

luminol in the presence of peroxidase of potato tissue to generate CL signal. The detection limit was 5.3 × 10−8 g ml−1 and the biosensor was applied to monitor the variation of dopamine level in the blood of rabbit after the administration of dopamine, combined with microdialysis sampling. 3.3.4. Isoniazid CL sensors A CL sensor for isoniazid was developed based on its enhancement to weak CL reaction between luminol and periodate [71]. Both reagents were electrostatically immobilized on anion exchange resin. The detection limit was 4.2 × 10−9 mol l−1 isoniazid. Other authors found that isoniazid could inhibit the CL reaction between luminol and ferricyanide. A CL sensor based on the inhibiting effect was also developed with the detection limit of 0.35 ng ml−1 isoniazid [72]. 3.3.5. Ofloxacin CL sensors The sensitizing effect of ofloxacin on the CL oxidation of sulfite by PbO2 in H2 SO4 media has been applied for the design of CL ofloxacin sensor [24]. The detection limit was 7.8 × 10−8 g ml−1 ofloxacin. 3.3.6. Pipemidic acid CL sensors The sensitizing effect of pipemidic acid on the CL oxidation of sulfite by sodium bismuthate was also studied [25]. The calibration graph is linear in the range 0.1−10 ␮g ml−1 with a detection limit of 6.2 × 10−8 g ml−1 . KMnO4 was also applied for the design of pipemidic acid CL sensor based on its strong oxidation property [73]. Furthermore, the CL sensor was successfully combined with ultrafiltration sampling and applied to study in vitro the bovine serum album (BSA) binding of pipemidic acid. The method provided a fast and simple technique for the study of drug–protein interaction. 3.3.7. Reserpine, novalgin and berberine CL sensors All these CL sensors reported in literature were based on the inhibition effect to CL reaction. For example, the CL emissions from luminol and dichromate could be greatly suppressed by novalgin [74] and reserpine [75]. The detection limits for both drugs were 2.0 × 10−11 and 0.4 × 10−9 g ml−1 , respectively. Similar inhibition effect of reserpine on luminol–periodate reaction [76] and berberine on luminol–potassium ferricyanide reaction [77] were also reported. The detection limits for both drugs were 0.3 and 0.02 ng ml−1 , respectively. 3.3.8. Pesticide or herbicide CL sensors Several CL sensors were developed recently for the determination of pesticide and herbicide based on immunoassays. For example, a heterogeneous 1,1,1-trichloro-2,2-bis(pchlorphenyl)ethane (DDT) CL sensor has been developed by Botchkareva et al. [78] based on enzyme-labeled specific monoclonal antibodies (MAbs). The enhanced lumi-

44

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

Table 2 CL sensors for organic and biological compounds Analyte 1,10-Phenanthroline 2,4-D 2,4-D 3-Hydroxybutyrate

Acetylcholine Acetylcholine Adrenaline Alpha-ketoglutarate Amygdalin Analgin Analgin Analgin Atropine Berberine Biological pollutants Butanone Chlorpyrifos Choline Choline Choline Cholesterol Codeine d-Amino DDT Dopamine Ethanol Ethanol Ethanol Ethanol Folic acid Formaldehyde Fragrance Gallic acid Glucose Glucose Glucose Glucose Glucose Glucose

Glucose Glycolic Acid Histamine Hydrocarbon Isoniazid Isoniazid Isoprenaline Lactate

CL reaction system H2 O2 –1,10–phenanthroline Luminol–H2 O2 –p-iodophenol–HRP labelled 2,4-D Luminol–H2 O2 –p-iodophenol–HRP labelled 2,4-D antibody 3-Hydroxybutyrate dehydrogenase–glucose dehydrogenase–NADH oxidase–peroxidase–luminol Acetylcholinesterase–luminol–hexacyanoferrate Acetylcholinesterase and HRP Periodate–luminol–adrenaline alanine Aminotransferase–glutamate oxidase–peroxidase–luminol–Co2+ Luminol–beta-glucosidase–luminol Dissovled O2 –analgin–R6G Periodate–luminol–analgin Manganese dioxide–analgin–R6G Ru(bipy)3 2+ –Ce(SO4 )2 Potassium ferricyanide–luminol–berberine Luminol–H2 O2 –HRP O2 –butanone–Mg2 AlO7/2 Periodate–luminol–reserpine Choline oxidase–luminol–hexacyanoferrate Choline oxidase and HRP modified with histidine Choline oxidase and HRP Cholesterol oxidase–luminol–ferricyanide Ruthenium(II) complex–Ce4+ O2 –d-amino–d-amino acid oxidase–luminol–ferricyanide Luminol/H2 O2 /p-iodophenol–HRP labeled antibodies Oxygen–dopamine–polyphenol oxidase–luminol–peroxidase O2 –ethanol–nanosized TiO2 O2 –ethanol–nanosized SrCO3 O2 –ethanol–nanosized ZrO2 Ru(bpy)3 2+ –KMnO4 or Ce(SO4 )2 Hexacyanoferrate–luminol–folic acid KIO4 –luminol–formaldehyde O2 –fragrance–␥-Al2 O3 /Dy3+ Periodate–luminol–gallic acid O2 –glucose–HRP,GOD–luminol O2 –glucose–GOD–luminol–ferricyanide O2 –glucose–glucose oxidase–luminol–Co(II)–ethanolamine complex O2 –glucose–GOx–luminol Glucose oxidase–luminol–potassium ferricyanide 3-hydroxybutyrate dehydrogenase–glucose dehydrogenase–NADH oxidase–peroxidase–luminol O2–glucose–glucose oxidase–Luminol–potassium ferricyanide Oxygen–glycolic acid–glycolate oxidase–luminol–H2 O2 –peroxidase Histamine oxidase–luminol–peroxidase O2 –hydrocarbon–␥-Al2 O3 /Dy3+ Luminol–periodate–isoniazid Luminol–ferricyanide–isoniazid Periodate–luminol–isoprenaline O2 –lactate–lactate oxidase–luminol–ferricyanic

Linear range 0.5–5000 ng ml−1 4–160 mg l−1

Detection limit

Reference

4 × 10−6

50 pg ml−1

[17] [80]

4 mg l−1

[79]

mol dm−3

0.05–10 nM 6 × 10−8 to 1 × 10−4 M 3–3000 nM 2.0 × 10−8 to 1.0 × 10−5 g ml−1 Over two decades 1.0–200 ng 0.4–10 mg l−1 0.1–50.0 ng ml−1 4 × 10−5 to 1 × 10−3 g/ml Over three orders 0.05–300 ng ml−1 16.5–66 ng/1 m3 20–1000 mg m−3 0.48–484.0 ng ml−1 4 × 10−8 to 1 × 10−4 M 0.35 pmol to 10 nmol 1–1000 nM 5 × 10−6 to 1 × 10−4 g ml−1 1.1 × 10−6 to 1.1 × 10−4 M

1 × 10−7 to 1 × 10−5 g ml−1

[85]

1.2 pmol 7.0 × 10−9 g ml−1 5 nM 0.3 ng 0.15 mg l−1 0.04 ng ml−1 2.7 × 10−5 g/ml 3.8 × 10−9 0.02 ng ml−1

[57] [59] [56] [52]

6.2 mg m−3 0.18 ng ml−1 0.03 pmol 0.5 pmol

[86] [67] [68] [23] [87] [88] [66] [21] [89] [57] [58]

5 × 10−6 g ml−1 1 × 10−8 M 4.5 × 10−7 M

[59] [90] [91] [49]

1 nM

[78]

5.3 × 10−8 g ml−1

[70]

40–400 ng ml−1 6–3750 ppm 1.6–160 ng ml−1 0.5% (v/v) 0.01–15 ng ml−1 5.0–1000.0 ng ml−1 0.1–1 ppm 8.0 × 10−9 to 1.0 × 10−6 mol l−1 0–12 mM 1.1–110 mM 1.0 × 10−6 to 1 × 10−4 M

6.5 × 10−9 mol l−1 0.05 mM 0.1 mM 1 × 10−6 M

[18] [20] [19] [11] [92] [93] [94] [95] [96] [62] [30]

Over three decades 3.5–70 nM

7.5 nM 0.6 nM

[33] [97]

2.1 ppm 0.6 ng ml−1 3.5 ng ml−1 1.8 ng ml−1

0.1–30 nM

[81]

0.0003–0.05 mM

[98]

4 × 10−6 to 4 × 10−3 M 0.1–50 nM 0.2–1000 ppm 8.0 × 10−9 to 1.0 × 10−6 mol l−1 0.001–1.0 mg ml−1 2.0 × 10−7 to 5.0 × 10−5 gml−1 0.5 and 5.0 mM

1.3 × 10−6 M

4.2 × 10−9 mol l−1 0.35 ng ml−1 5.0 × 10−8 g ml−1

[15] [99] [100] [71] [72] [101]

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

45

Table 2 (Continued) Analyte

CL reaction system

Linear range

Detection limit

Reference

l-Alanine

Alanine aminotransferase and glutamate oxidase–luminol–Co(II) ions, peroxidase l-Aspartate–aspartate, aminotransferase and l-glutamate oxidase–luminol–peroxidase Alanine aminotransferase and glutamate oxidase–luminol–Co(II) ions, peroxidase l-Glutamate–glutamate oxidase–uricase–peroxidase–luminol Glutamate oxidase/peroxidase Lysine oxidase/peroxidase Periodate–luminol–lysozyme Luminol–H2 O2 –p-iodophenol–HRP labeled antibodies Ru(bpy)3 2+ –KMnO4 or Ce(SO4 )2 Ru(bipy)3 2+ –Ce(SO4 )2 Sodium bismuthate–sulfite–pipemidic acid KMnO4 –sulfite–pipemidic acid Dichromate–luminol–reserpine Periodate–luminol–reserpine Periodate–luminol–riboflavin Hexacyanoferrate–luminol–rutin Ru(bpy)3 2+ –KMnO4 or Ce(SO4 )2 Peroxidase–luminol–H2 O2 Urea–urease–permanganate–luminol Uric acid–Uricase–TCPO–rubrene Uric acid–luminol–periodate Dissolved O2 –Vitamin K-3–R6G KMnO4 –organic compounds–luminol Phosphatase labelled DNA probe–AMPPD substrate Phosphatase labelled DNA probe–AMPPD substrate HRP-labeled complementary nucleotides–luminol–H2 O2 H2 O2 –luminol–antioxidants–hematin

Over two decades

2 nM

[52]

l-Aspartate l-Glutamate l-Glutamate l-Glutamate L-Lysine Lysozyme Okadaic acid Oxalate Pethidine Pipemidic acid Pipemidic acid Reserpine Reserpine Riboflavin Rutin Sulfite terbutylazine Urea Uric acid Uric acid Vitamin K-3 chemical Oxygen demand DNA Nucleic acids DNA Antioxidants

5–1000 mM

[50]

Over two decades

1 nM

[52]

5–20 nM

10 nM

[51]

40–1000 nM 50–1200 nM 30–1000 ng ml−1 0.2–200 mg/100 g

20 nM 40 nM 0.2 mg/100 g

[102] [102] [103] [104]

6.2 × 10−8 g ml−1 1.6 × 10−7 mol l−1 0.4 ng ml−1 0.3 ng ml−1 0.02 ng ml−1 0.35 ng ml−1 1 × 10−7 M 20 ng l−1 2 mM 5 ␮M 1.8 ng ml−1 2.6 ng l−1 . 2 mg l−1 3 × 10−14 mol l−1

[11] [105] [25] [73] [75] [106] [54] [107] [11] [108] [14] [60] [61] [53] [109] [64]

15 pM

[63]

0.1 ppm

[65]

100 nM

[110]

1 × 10−6 M 7.7 × 10−8 M 0.1–10 ␮g/ml 3.4 × 10−7 to 3.4 × 10−5 mol l−1 1.0–500.0 ng ml−1 1.0–300 ng ml−1 0.04–200 ng ml−1 1.0–400 ng ml−1

4–400 mM 0.01–1 mM 5.0–500.0 ng ml−1 0.5–10 ng ml−1 4–4000 mg l−1

Five orders of magnitude

1 × 10−4 to 0.10 M

MP: maltose phosphorylase; MUT: mutarotase; GOD: glutamate oxidase; R6G: rhodamine 6G; GOx: glucose oxidase; NADH: nicotinamid adenin dinucleotid hydroeen; TCPO: 2,4,6-(trichlorophenyl)-oxalate; AMPPD: 3-(2 -spiroadamantane)-4-methoxy-4-(3 -phosphoryloxy) phenyl-1,2-dioxetane.

nescent detection (luminol/H2 O2 /p-iodophenol) was used through the detection. The lowest limit of detection of 1 nM p,p-DDT was obtained. A semi-automated CL competitive immunosensor for the herbicide 2,4-dichlorophenoxyacetic acid (2,4-D) has been developed by Marquette and Blum [79]. Anti-2,4-D polyclonal antibodies were directly labeled with horseradish peroxidase allowing a p-iodophenol enhanced CL detection. Such a sensor enables the detection of 4 mg l−1 of free antigen and the 2,4-D detection was possible in the range 4–160 mg l−1 . Another 2,4-D CL sensor was investigated by Danielsson et al. [80] based on competition between the binding of HRP labeled versus unlabeled 2,4-D, on immobilized anti-2,4-D monoclonal antibodies (mAbs). Two other peroxidases from tomato (MOP) and tobacco (TOP) were also employed as labels for the 2,4-D assays. TOP demonstrated a higher specific activity compared to MOP and HRP. A detection limit of 50 pg ml−1 for 2,4-D was obtained using TOP conjugate and CL detection. Table 2 gives the summary of CL sensors developed for organic and biological compounds.

4. Conclusions Owing to the property of extremely high sensitivity along with the simple instrumentation, fast dynamic response properties, and wide calibration ranges, CL sensor is continually received more and more attentions in recent years. Much effort has been devoted to the improvement of lifetime of CL sensors by reducing the consumption of reagents. However, the consumption of reagents was generally accompanied with CL reactions, and results in the deterioration of the indicator phases or the sensors on prolonged use. This is the reason why the lifetime is still a blockage of the practical application of the CL sensor. Further developments would be focused on the improvement of the lifetime of this type of sensors, and on the improvement of selectivity by careful selection of suitable CL reaction systems. Miniaturization of CL sensors for special applications should also be studied so as to extend this new technique to life sciences as well as to other areas. High attention should be paid to the development of CL sensors based on new technologies in order to take a breakthrough

46

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47

in sensing mechanism. The molecular imprinting technique should be further studied for its high selectivity. CL sensors based on nanosized materials would be a hot research point, which would offer new opportunities to construct miniaturized CL sensor with long lifetime, as demonstrated by recent publications.

Acknowledgement We gratefully acknowledge financial support of the work by National Natural Science Foundation of China (Nos. 20375022 and 20345005).

References [1] X.R. Zhang, W.R.G. Baeyens, A.M. Garc´ıa-Campa˜na, J. Ouyang, Trac-Trend. Anal. Chem. 18 (1999) 384–391. [2] H.Y. Aboul-Enein, R.I. Stefan, J.F. van Staden, X.R. Zhang, A.M. Garc´ıa-Campa˜na, W.R.G. Baeyens, Crit. Rev. Anal. Chem. 30 (2000) 271–289. [3] A.M. Garc´ıa-Campa˜na, W.R.G. Baeyens, Chemiluminescence in Analytical Chemistry, Marcel Dekker, NY, 2001, pp. 567–591. [4] W. Qin, Z.J. Zhang, Anal. Lett. 30 (1997) 11–19. [5] J.Z. Lu, W. Qin, Z.J. Zhang, M.L. Feng, Y.J. Wang, Anal. Chim. Acta 304 (1995) 369–373. [6] J.Z. Lu, Z.J. Zhang, Huaxue Xuebao 54 (1996) 71–76. [7] W. Qin, Z.J. Zhang, Fresenius J. Anal. Chem. 361 (1998) 824–826. [8] Z.J. Zhang, W. Qin, Talanta 43 (1996) 119–124. [9] W. Qin, Z.J. Zhang, B.X. Li, S.N. Liu, Anal. Chim. Acta 372 (1998) 357–363. [10] B.X. Li, W. Qin, Z.J. Zhang, Chin. Chem. Lett. 9 (1998) 471–472. [11] J.M. Lin, F. Qu, M. Yamada, Anal. Bioanal. Chem. 374 (2002) 1159–1164. [12] K.M. Wang, J. Li, X.H. Yang, F.L. Shen, X. Wang, Sens. Actuators B: Chem. 65 (2000) 239–240. [13] B.X. Li, Z.J. Zhang, L.X. Zhao, Anal. Chim. Acta 445 (2001) 161–167. [14] W. Qin, Z.J. Zhang, Y.Y. Peng, Anal. Chim. Acta 407 (2000) 81–86. [15] B.X. Li, Z.J. Zhang, Y. Jin, Anal. Chem. 73 (2001) 1203–1206. [16] J.M. Lin, M. Yamada, Anal. Chem. 72 (2000) 1148–1155. [17] J.M. Lin, M. Yamada, Analyst 126 (2001) 810–815. [18] Y.F. Zhu, J.J. Shi, Z.Y. Zhang, C. Zhang, X.R. Zhang, Anal. Chem. 74 (2002) 120–124. [19] Z.Y. Zhang, C. Zhang, X.R. Zhang, Analyst 127 (2002) 792–796. [20] J.J. Shi, J.J. Li, Y.F. Zhu, F. Wei, X.R. Zhang, Anal. Chim. Acta 466 (2002) 69–78. [21] K.W. Zhou, X.R. Zhang, Chin. J. Anal. Chem. 32 (2004) 25–28. [22] X.O. Cao, Z.Y. Zhang, X.R. Zhang, Sens. Actuators B: Chem. 99 (2004) 30–35. [23] L.X. Zhao, B.X. Li, Z.J. Zhang, J.M. Lin, Sens. Actuators B: Chem. 97 (2004) 266–271. [24] B.X. Li, Z.J. Zhang, L.X. Zhao, C.L. Xu, Talanta 57 (2002) 765–771. [25] B.X. Li, Z.J. Zhang, L.X. Zhao, C.L. Xu, Anal. Chim. Acta 459 (2002) 19–24. [26] G.J. Zhou, G. Wang, J.J. Xu, H.Y. Chen, Sens. Actuators B: Chem. 81 (2002) 334–339. [27] D. Janasek, U. Spohn, A. Kiesow, A. Heilmann, Sens. Actuators B: Chem. 78 (2001) 228–231. [28] O. Nozaki, H. Kawamoto, Anal. Chim. Acta 495 (2003) 233–238.

[29] P. Qu, B.X. Li, Z.J. Zhang, Chin. J. Anal. Chem. 31 (2003) 1240–1243. [30] J.M. Lin, X.Q. Shan, S. Hanaoka, M. Yamada, Anal. Chem. 73 (2001) 5043–5051. [31] S. Hanaoka, J.M. Lin, M. Yamada, Anal. Chim. Acta 426 (2001) 57–64. [32] N. Kiba, T. Tokizawa, S. Kato, M. Tachibana, K. Tani, H. Koizumi, M. Edo, E. Yonezawa, Anal. Sci. 19 (2003) 823–827. [33] C.A. Marquette, L.J. Blum, Anal. Lett. 36 (2003) 1697–1706. [34] W. Qin, Z.J. Zhang, B.X. Li, Y.Y. Peng, Talanta 48 (1999) 225– 229. [35] H. Nakamura, H. Tanaka, M. Hasegawa, Y. Masuda, Y. Arikawa, Y. Nomura, K. Ikebukuro, I. Karube, Talanta 50 (1999) 799–807. [36] H. Nakamura, M. Hasegawa, Y. Nomura, Y. Arikawa, R. Matsukawa, K. Ikebukuro, I. Karube, J. Biotechnol. 75 (1999) 127–133. [37] H. Nakamura, M. Hasegawa, Y. Nomura, K. Ikebukuro, Y. Arikawa, I. Karube, Anal. Lett. 36 (2003) 1805–1817. [38] I.P.A. Morais, M. Mir´o, M. Manera, J.M. Estela, V. Cerd`a, M.R.S. Souto, A.O.S.S. Rangel, Anal. Chim. Acta 506 (2004) 17–24. [39] Y.M. Huang, C. Zhang, X.R. Zhang, Z.J. Zhang, Anal. Lett. 32 (1999) 1211–1224. [40] T. Takayanagi, X.L. Su, P.K. Dasgupta, K. Martinelango, G.G. Li, R.S. Al-Horr, R.W. Shaw, Anal. Chem. 75 (2003) 5916–5925. [41] C. Eipel, P. Jeroschewski, I. Steinke, Anal. Chim. Acta 491 (2003) 145–153. [42] V. Yushkov, A. Oulanovsky, N. Lechenuk, I. Roudakov, K. Arshinov, F. Tikhonov, L. Stefanutti, F. Ravegnani, U. Bonafe, T. Georgiadis, J. Atmos. Ocean Technol. 16 (1999) 1345–1350. [43] C.A.M. Brenninkmeijer, P.J. Crutzen, H. Fischer, H. Gusten, W. Hans, G. Heinrich, J. Heintzenberg, M. Hermann, T. Immelmann, D. Kersting, M. Maiss, M. Nolle, A. Pitscheider, H. Pohlkamp, D. Scharffe, K. Specht, A. Wiedensohler, J. Atmos. Ocean Technol. 16 (1999) 1373–1383. [44] D.C. Yao, M.I. Prodromidis, A.G. Vlessidis, M.I. Karayannis, N.P. Evmiridis, Anal. Chim. Acta 450 (2001) 63–72. [45] D.C. Yao, A.G. Vlessidis, N.P. Evmiridis, A. Evangelou, S. Karkabounas, S. Tsampalas, Anal. Chim. Acta 458 (2002) 281–289. [46] J.J. Shi, R.X. Yan, Y.F. Zhu, X.R. Zhang, Talanta 6 (2003) 157–164. [47] Z.H. Song, L. Wang, T.Z. Zhao, Anal. Lett. 34 (2001) 399–413. [48] M.M. Nakamura, N. Coichev, J.M. Lin, M. Yamada, Anal. Chim. Acta 484 (2003) 101–109. [49] B.X. Li, Z.J. Zhang, Sens. Actuators B: Chem. 69 (2000) 70–74. [50] D. Janasek, U. Spohn, Sens. Actuators B: Chem. 74 (2001) 163–167. [51] N. Kiba, S. Ito, M. Tachibana, K. Tani, H. Koizumi, Anal. Sci. 17 (2001) 929–933. [52] D. Janasek, U. Spohn, Biosens. Bioelectron. 14 (1999) 123–129. [53] Y.M. Huang, Z.Q. Chen, Z.J. Zhang, Anal. Sci. 15 (1999) 1227–1230. [54] Z.H. Song, L. Wang, Analyst 126 (2001) 1393–1398. [55] Y.M. Huang, C. Zhang, Z.J. Zhang, Anal. Sci. 15 (1999) 867–870. [56] G.J. Zhou, G.F. Zhang, H.Y. Chen, Anal. Chim. Acta 463 (2002) 257–263. [57] D. Yao, A.G. Vlessidis, N.P. Evmiridis, Anal. Chim. Acta 462 (2002) 199–208. [58] V.C. Tsafack, C.A. Marquette, F. Pizzolato, L.J. Blum, Biosens. Bioelectron. 15 (2000) 125–133. [59] N. Kiba, S. Ito, M. Tachibana, K. Tani, H. Koizumi, Anal. Sci. 19 (2003) 1647–1651. [60] D.C. Yao, A.G. Vlessidis, N.P. Evmiridis, Anal. Chim. Acta 478 (2003) 23–30. [61] Z.H. Song, S. Hou, Anal. Bioanal. Chem. 372 (2002) 327–332. [62] Y. Lv, Z.J. Zhang, F.N. Chen, Talanta 59 (2003) 571–576. [63] D.K. Xu, L.R. Ma, Y.Q. Liu, Z.H. Jiang, Z.H. Liu, Analyst 124 (1999) 533–536. [64] X.P. Jiang, D.K. Xu, Y.Q. Liu, L.R. Ma, Chin. J. Anal. Chem. 28 (2000) 12–16.

Z. Zhang et al. / Analytica Chimica Acta 541 (2005) 37–47 [65] G.J. Zhang, Y.K. Zhou, J.W. Yuan, S. Ren, Anal. Lett. 32 (1999) 2725–2736. [66] V.M. Starodub, L.L. Fedorenko, N.F. Starodub, Sens. Actuators B: Chem. 68 (2000) 40–47. [67] Y.M. Huang, C. Zhang, X.R. Zhang, Z.J. Zhang, Fresenius J. Anal. Chem. 365 (1999) 381–383. [68] Z.H. Song, N. Zhang, Bioorg. Med. Chem. 10 (2002) 2091–2097. [69] B.G. Knecht, A. Strasser, R. Dietrich, E. Martlbauer, R. Niessner, M.G. Weller, Anal. Chem. 76 (2004) 646–654. [70] B.X. Li, Z.J. Zhang, Y. Jin, Biosens. Bioelectron. 17 (2002) 585–589. [71] S.C. Zhang, H. Li, Anal. Chim. Acta 444 (2001) 287–294. [72] Z.H. Song, J.H. Lu, T.Z. Zhao, Talanta 53 (2001) 1171–1177. [73] B.X. Li, Z.J. Zhang, L.X. Zhao, Anal. Chim. Acta 468 (2002) 65–70. [74] Z. Song, N. Zhang, Talanta 60 (2003) 161–170. [75] Z.H. Song, N. Zhang, Chin. J. Chem. 21 (2003) 175–180. [76] Z.H. Song, N. Zhang, Anal. Lett. 36 (2003) 41–57. [77] Z.H. Song, T.Z. Zhao, L. Wang, Z. Xiao, Bioorg. Med. Chem. 9 (2001) 1701–1705. [78] A.E. Botchkareva, F. Fini, S. Eremin, J.V. Mercader, A. Montoya, S. Girotti, Anal. Chim. Acta 453 (2002) 43–52. [79] C.A. Marquette, L.J. Blum, Talanta 51 (2000) 395–401. [80] B. Danielsson, I. Surugiu, A. Dzgoev, M. Mecklenburg, K. Ramanathan, Anal. Chim. Acta 426 (2001) 227–234. [81] M.C. Cheregi, J.V.G. Mateo, J.M. Calatayud, A.F. Danet, Revista De Chimie 50 (1999) 325–336. [82] G.H. Liu, Y.F. Zhu, X.R. Zhang, B.Q. Xu, Anal. Chem. 74 (2002) 6279–6284. [83] B.X. Li, Z.J. Zhang, Y. Jin, Sens. Actuators B: Chem. 72 (2001) 115–119. [84] M.J. Robinson, J.W. Bollinger, Birks, Anal. Chem. 71 (1999) 5131–5136. [85] N. Kiba, Y. Inoue, M. Tachibana, K. Tani, H. Koizumi, Anal. Sci. 19 (2003) 1203–1206. [86] Z.H. Song, Z.J. Zhang, Chin. J. Anal. Chem. 28 (2000) 964–967. [87] P.A. Greenwood, C. Merrin, T. McCreedy, G.M. Greenway, Talanta 56 (2002) 539–545. [88] Z.H. Song, T.Z. Zhao, L. Wang, Z. Xiao, Bioorg. Med. Chem. 9 (2001) 1701–1705.

47

[89] Z.G. Song, S.A. Hou, N. Zhang, J. Agric. Food Chem. 50 (2002) 4468–4474. [90] Y.M. Huang, C. Zhang, Z.J. Zhang, Anal. Sci. 15 (1999) 867– 870. [91] N.W. Barnett, R. Bos, H. Brand, P. Jones, K.F. Lim, S.D. Purcell, R.A. Russell, Analyst 127 (2002) 455–458. [92] Z.H. Song, X. Zhou, Spectrochim. Acta A 57 (2001) 2567–2574. [93] Z.H. Song, S.A. Hou, Int. J. Environ. Anal. Chem. 83 (2003) 807–817. [94] T. Okabayashi, T. Toda, I. Yamamoto, K. Utsunomiya, N. Yamashita, M. Nakagawa, Sens. Actuators B: Chem. 74 (2001) 152–156. [95] S.C. Zhang, G.J. Zhou, H.X. Ju, Chin. J. Chem. 20 (2002) 1049–1054. [96] B.X. Li, Z.J. Zhang, Y. Jin, Anal. Chim. Acta 432 (2001) 95–100. [97] Q.W. Li, Y.M. Wang, X.R. Zhang, G.A. Luo, Chin. J. Anal. Chem. 27 (1999) 1274–1277. [98] A.F. Danet, C. Velea, D. Murarau, Revista De Chimie 54 (2003) 867–870. [99] Y. Sekiguchi, A. Nishikawa, H. Makita, A. Yamamura, K. Matsumoto, N. Kiba, Anal. Sci. 17 (2001) 1161–1164. [100] T. Okabayashi, T. Fujimoto, I. Yamamoto, K. Utsunomiya, T. Wada, Y. Yamashita, N. Yamashita, M. Nakagawa, Sens. Actuators B: Chem. 64 (2000) 54–58. [101] H. Nakamura, Y. Murakami, K. Yokoyama, E. Tamiya, I. Karube, M. Suda, S. Uchiyama, Anal. Chem. 73 (2001) 373–378. [102] N. Kiba, T. Miwa, M. Tachibana, K. Tani, H. Koizumi, Anal. Chem. 74 (2002) 1269–1274. [103] Z.H. Song, S.A. Hou, Anal. Sci. 19 (2003) 347–352. [104] C.A. Marquette, P.R. Coulet, L.J. Blum, Anal. Chim. Acta 398 (1999) 173–182. [105] N.W. Barnett, R. Bos, H. Brand, P. Jones, K.F. Lim, S.D. Purcell, R.A. Russell, Analyst 127 (2002) 455–458. [106] Z.H. Song, N. Zhang, Anal. Lett. 36 (2003) 41–57. [107] Z.H. Song, L. Wang, J. Agric. Food Chem. 49 (2001) 5697–5701. [108] M.G. Weller, A.J. Schuetz, M. Winklmair, R. Niessner, Anal. Chim. Acta 393 (1999) 29–41. [109] B.X. Li, Z.J. Zhang, J. Wang, C.L. Xu, Talanta 61 (2003) 651–658. [110] W.S. Palaroan, J. Bergantin, F. Sevilla, Anal. Lett. 33 (2000) 1797–1810.