Ultrasensitive optical detection of hydrogen peroxide by triggered activation of horseradish peroxidase

Virel, Ana; Saá, Laura; Köster, S. David; Pavlov, Valeri

doi:10.1039/c0an00095g

Cited by 13 publications

(6 citation statements)

References 40 publications

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“…The majority of studies on HRP in biosensor systems focuses on the detection of H 2 O 2 (e.g. Kafi et al 2008 ; Virel et al 2010 ; Zhong et al 2011 ; Ahammad et al 2011 ). In recent years however, a considerable number of studies also dealt with the detection of other molecules, such as glucose (Alonso-Lomillo et al 2005 ), ethanol (Azevedo et al 2005 ), DNA and RNA (Fan et al 2013 ; Tran et al 2014 ; Saikrishnan et al 2014 ), l -phenylalanine (Kubota et al 2013 ), citrinin (Zachetti et al 2013 ), pyrogallol and hydroquinone (Raghu et al 2013 ), phenols (Kafi and Chen 2009 ; Liu et al 2011 ), the milk allergen β-lactoglobulin (Ruiz-Valdepeñas Montiel et al 2015 ), rotavirus titers (Li et al 2014 ), and tumor markers (Chen et al 2009 ; Kim et al 2014b ; Patris et al 2014 ) via H 2 O 2 .…”

Section: Impact Of Recombinant Technology On Traditional and Future Hmentioning

confidence: 99%

An updated view on horseradish peroxidases: recombinant production and biotechnological applications

Krainer

Glieder

2015

Appl Microbiol Biotechnol

186

133

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Horseradish peroxidase has been the subject of scientific research for centuries. It has been used exhaustively as reporter enzyme in diagnostics and histochemistry and still plays a major role in these applications. Numerous studies have been conducted on the role of horseradish peroxidase in the plant and its catalytic mechanism. However, little progress has been made in its recombinant production. Until now, commercial preparations of horseradish peroxidase are still isolated from plant roots. These preparations are commonly mixtures of various isoenzymes of which only a small fraction has been described so far. The composition of isoenzymes in these mixed isolates is subjected to uncontrollable environmental conditions. Nowadays, horseradish peroxidase regains interest due to its broad applicability in the fields of medicine, life sciences, and biotechnology in cancer therapy, biosensor systems, bioremediation, and biocatalysis. These medically and commercially relevant applications, the recent discovery of new natural isoenzymes with different biochemical properties, as well as the challenges in recombinant production render this enzyme particularly interesting for future biotechnological solutions. Therefore, we reviewed previous studies as well as current developments with biotechnological emphasis on new applications and the major remaining biotechnological challenge—the efficient recombinant production of horseradish peroxidase enzymes.

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Section: Impact Of Recombinant Technology On Traditional and Future Hmentioning

confidence: 99%

An updated view on horseradish peroxidases: recombinant production and biotechnological applications

Krainer

Glieder

2015

Appl Microbiol Biotechnol

186

133

View full text Add to dashboard Cite

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“…Based on this phenomenon, we developed a new facile colorimetric method for glucose detection with the CeO 2 NPs as peroxidase mimetics. Compared with various glucose sensors using horseradish peroxidase (HRP), [29][30][31] this method with CeO 2 NPs as peroxidase mimetics has numerous advantages including high stability, low-cost, and ease of preparation. Furthermore, this method is used for glucose detection in human blood serum samples; the results indicate that the highly sensitive and selective glucose detection method has a wide range of potential applications in bioanalysis.…”

Section: Introductionmentioning

confidence: 99%

Well-redispersed ceria nanoparticles: Promising peroxidase mimetics for H2O2 and glucose detection

et al. 2012

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Well-redispersed ceria nanoparticles (CeO 2 NPs) were synthesized by a simple hydrothermal method. The prepared CeO 2 NPs exhibited excellent catalytic activity towards classical peroxidase substrate 3,3,5,5-tetramethylbiphenyl dihydrochloride (TMB$2HCl) in the presence of H 2 O 2 , based on which a colorimetric method that is highly sensitive and selective was developed for glucose detection. The composition, structure, morphology and peroxidase-like catalytic activity of CeO 2 NPs are investigated in detail by using X-ray diffraction (XRD), transmission electron microscopy (TEM), high resolution transmission electron microscopy (HRTEM), selected area electron diffraction (SAED), X-ray photoelectron spectroscopy (XPS), Fourier transform infrared spectrometer (FT-IR), thermal analysis (TG) and UV-vis absorption spectroscopy. According to this method, the detection of H 2 O 2 and glucose are in linear range from 6.0 Â 10 À7 to 1.5 Â 10 À6 mol L À1 and 6.6 Â 10 À6 to 1.3 Â 10 À4 mol L À1 , with the detection limit down to 5.0 Â 10 À7 mol L À1 H 2 O 2 and 3.0 Â 10 À6 mol L À1 glucose, respectively. Further, this simple, cheap, highly sensitive and selective colorimetric method for glucose detection was successfully applied for the determination of glucose in human serum samples.

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“…In numerous cases, this enzyme activation process, also termed enzyme reconstitution, can be achieved in vitro through a precise control of the reaction conditions (temperature, buffer composition, pH …), paving thus the way for fundamental investigations of enzyme structure/reactivity relationships (notably by taking advantage of engineered binding partners such as apoenzyme mutants and/or cofactor analogs) 1,2,3,4,5,6,7,8 or even for discovering new enzyme functionalities. 9,10,11 Besides to the capacity of switching on the activity of an enzyme by simply adding its cofactor, enzyme reconstitution has also been advantageously exploited in different biotechnological applications, 5,10,12,13,14,15,16,17,18,19 ranging from the design of artificial signal transduction systems for analytical purposes to the development of new applications in biotechnology, bioelectronics or synthetic biology. 10,20,21,22,23,24,25 Among the enzymes whose catalytic activity can be easily and efficiently switched on via reconstitution, the soluble quinoprotein glucose dehydrogenase (sGDH, code UniprotKB F0KFV3) is certainly the most prevailing and attractive.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of Reconstitution/Activation of the Soluble PQQ-Dependent Glucose Dehydrogenase from Acinetobacter calcoaceticus: A Comprehensive Study

et al. 2020

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The ability to switch on the activity of an enzyme through its spontaneous reconstitution has proven to be a valuable tool in fundamental studies of enzyme structure/reactivity relationships or in the design of artificial signal transduction systems in bioelectronics, synthetic biology, or bioanalytical applications. In particular, those based on the spontaneous reconstitution/activation of the apo-PQQ-dependent soluble glucose dehydrogenase (sGDH) from Acinetobacter calcoaceticus were widely developed. However, the reconstitution mechanism of sGDH with its two cofactors, i.e. the pyrroloquinoline quinone (PQQ) and Ca 2+ , remains unknown. The objective here is to elucidate this mechanism by stopped-flow kinetics under single-turnover conditions. The reconstitution of sGDH exhibited biphasic kinetics, characteristic of a square reaction scheme associated to two activation pathways. From a complete kinetic analysis, we were able to fully predict the reconstitution dynamic, but also to demonstrate that when PQQ first binds to the apo-sGDH, it strongly impedes the access of Ca 2+ to its enclosed position at the bottom of the enzyme binding site, thereby greatly slowing down the reconstitution rate of sGDH. This slow calcium insertion may purposely be accelerated by providing more flexibility to the Ca 2+ binding loop through the specific mutation of the calcium coordinating P248 proline residue, reducing thus the kinetic barrier to calcium ion insertion. The dynamic nature of the reconstitution process is also supported by the observation of a clear loop shift and a reorganization of the hydrogen bonding network and van der Waals interactions observed in both active sites of the apo and holo forms, a structural change modulation that was revealed from the refined X-ray structure of apo-sGDH (PDB:5MIN).

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Ultrasensitive optical detection of hydrogen peroxide by triggered activation of horseradish peroxidase

Cited by 13 publications

References 40 publications

An updated view on horseradish peroxidases: recombinant production and biotechnological applications

An updated view on horseradish peroxidases: recombinant production and biotechnological applications

Well-redispersed ceria nanoparticles: Promising peroxidase mimetics for H2O2 and glucose detection

Mechanism of Reconstitution/Activation of the Soluble PQQ-Dependent Glucose Dehydrogenase from Acinetobacter calcoaceticus: A Comprehensive Study

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