Horseradish peroxidase functionalized gold nanorods as a label for sensitive electrochemical detection of alpha-fetoprotein antigen
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Horseradish peroxidase
Differential pulse voltammetry
Nanorod
Linear range
Differential pulse voltammetry
Linear range
Electrochemical gas sensor
Nanochemistry
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Horseradish peroxidase
Differential pulse voltammetry
Nanorod
Linear range
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Linear range
Nanorod
Silver nanoparticle
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The objective of the present work was to examine biocatalytic properties of peroxidase in horseradish acclimatized in our country. We have found that horseradish root extract’s peroxidase (HRP) has Km 2.5 mM and Vmax 5.36 mM·s-1. Maximum activity (pHopt) was estimated at pH 6.0 and enzyme is more stable in alkali, than in acid. The optimum temperature (Topt) for HRP is 40oC and the enzyme is not stable to temperature influence. The horseradish root’s extract retains enzymatic activity within 21 days. DOI: http://doi.dx.org/10.5564/mjc.v15i0.332 Mongolian Journal of Chemistry 15 (41), 2014, p101-103
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Horseradish peroxidase
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Simultaneous determination of erythromycin (Ery) and hemoglobin (Hb) is of great significance for clinical diagnosis of many diseases. ZnO nanorods modified with Au nanoparticles were fabricated as an interface on the flexible carbon cloth (CC) and utilized to simultaneously determine Ery and Hb by a simple electrochemical method. The results demonstrated that Au/ZnO/CC displayed excellent analytical performance for Ery with a low detection limit of 3.38 × 10−7 mg/L and a linear range from 1 × 10−6 to 1 × 10−1 mg/L. At the same time, the sensor also showed a sensitive response to Hb with a low detection limit of 2.07 × 10−7 mg/L and a linear range from 1 × 10−6 to 1 × 10−1 mg/L. This work provides a viable approach for designing a flexible electrode and sensitive simultaneous determination of Ery and Hb.
Nanorod
Differential pulse voltammetry
Linear range
Electrochemical gas sensor
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The present study describes an easy and efficient procedure for the purification of horseradish peroxidase from horseradish roots. For this purpose, supermacroporous cryogels having Concanavalin A were prepared by photosensitive cross-linking polymerization. Horseradish peroxidase binding and elution from the prepared cryogels were carried out changing various parameters such as initial peroxidase concentration and pH. The best binding performance was obtained at pH 7.0. The maximum horseradish peroxidase binding of the cryogels was found to be 3.85 mg g −1 cryogel. Horseradish peroxidase purification from crude extract resulted in 115.1-fold. SDS-PAGE analysis and circular dichroism measurements indicated that the horseradish peroxidase purification from horseradish roots was successfully carried out.
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A new method for the determination of horseradish per ox idase (HRP) was investigated by spectrophotometry based on 4-aminobiphenyl-H 2O 2-HRP system.It was based on H 2O 2 oxidation of 4-aminobiphenyl catalyz ed by HRP.When it was used in the determination of free HRP,the linear range was 3.0× 10 -10 ～8.0×10 -8g/mL,and the detection limit was 3.0× 10 -10g/mL.
Horseradish peroxidase
Spectrophotometry
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Thionine
Differential pulse voltammetry
Aptamer
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