Studies on Horseradish Peroxidase Immobilized onto Arylamine and Alkylamine Glass

Pundir, C.S.; Malik, Vinay; Bhargava, Ajay; Thakur, Manisha; Kalia, V; Singh, Santosh Kumar; Kuchhal, N. K.

doi:10.1007/bf03263073

Cited by 22 publications

(21 citation statements)

References 7 publications

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“…Normal levels of oxalate for a healthy human are 10 -30 mg/24 h (100 -300 μM) in urine 9 and 0.8 -2.50 μM in plasma. 10 A urinary oxalate concentration higher than 300 μM can indicate the occurrence of initial kidney stones. Kidney stones can cause renal function deterioration and kidney failure in endstage renal disease.…”

Section: Introductionmentioning

confidence: 99%

A Simple Paper-based Colorimetric Device for Rapid and Sensitive Urinary Oxalate Determinations

et al. 2018

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In this work, a simple and inexpensive paper-based colorimetric device (cPAD) was developed for oxalate measurements. The colorimetric assay is based on the formation of formazan via the reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) by oxalate decarboxylase and formate dehydrogenase on the paper device. After the sample was spotted on the device, MTT changed color from yellow to purple, and the purple color intensity correlated with the oxalate concentration. The quantitative detection of oxalate ranged from 10 -1000 μM, with a linear equation, y = 0.0086x + 34.978, and a correlation coefficient (R 2 ) = 0.9994. The detection limit was 10 μM by the naked eye. The recoveries of oxalate spiked in artificial urine samples evaluated by our cPADs were in the range of 81 -92%. This simple cPAD for rapid and sensitive oxalate determination should be useful for diagnostic urinary oxalate measurements for point-of-care monitoring.

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Section: Introductionmentioning

confidence: 99%

A Simple Paper-based Colorimetric Device for Rapid and Sensitive Urinary Oxalate Determinations

et al. 2018

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“…The horseradish peroxidase nanoparticles immobilized polyvinyl chloride vial was showed optimum activity at pH-7.2, which was higher as compared to the optimum pH of 7.0 for free enzyme [14]. Li and Townshend [15] was also reported different optimum pH for the peroxidase activity before (7.0) and after immobilization (5.8) on polytetrafluoroethylene tubing.…”

Section: Studied Kinetic Characterization Of Activated Plasticized Pomentioning

confidence: 92%

“…The optimum temperature for immobilized peroxidase nanoparticles was 40°C, as compared to free enzyme which shows optimum activity at 25°C [14]. This change signifies the protecting effect of support which might have stabilized the three dimensional structure of enzyme.…”

Section: Studied Kinetic Characterization Of Activated Plasticized Pomentioning

confidence: 96%

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A Cost Effective Immobilization of Horseradish Peroxidase Nanoparticles on to Easy-To-Prepare Activated Plasticized Polyvinyl-Chloride Vial and Its Application

Rani

Chauhan

Narang

et al. 2015

JNMR

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“…Many supports and methods have also been used for HRP immobilization: magnetite by physical adsorption [11], glass beads by different methods of covalent coupling [12][13][14], a wide variety of polymers in many diverse configurations [15][16][17][18][19], and ion exchange resins [20]. Some of these immobilized derivatives have been applied to 4-chlorophenol removal with promising results [11,14,15].…”

Section: Introductionmentioning

confidence: 98%

A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization

Bódalo

Bastida

Máximo

et al. 2008

Bioprocess Biosyst Eng

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Horseradish peroxidase (HRP) and soybean peroxidase (SBP) were covalently immobilized onto aldehyde glass through their amine groups. The activity yield and the protein content for the immobilized SBP were higher than for the immobilized HRP. When free and immobilized peroxidases were tested for their ability to remove 4-chlorophenol from aqueous solutions, the removal percentages were higher with immobilized HRP than with free HRP, whereas immobilized SBP needs more enzyme to reach the same conversion than free enzyme. In the present paper the two immobilized derivatives are compared. It was found that at an immobilized enzyme concentration in the reactor of 15 mg l(-1), SBP removed 5% more of 4-chlorophenol than HRP, and that a shorter treatment was necessary. Since immobilized SBP was less susceptible to inactivation than HRP and provided higher 4-chlorophenol elimination, this derivative was chosen for further inactivation studies. The protective effect of the immobilization against the enzyme inactivation by hydrogen peroxide was demonstrated.

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Studies on Horseradish Peroxidase Immobilized onto Arylamine and Alkylamine Glass

Cited by 22 publications

References 7 publications

A Simple Paper-based Colorimetric Device for Rapid and Sensitive Urinary Oxalate Determinations

A Simple Paper-based Colorimetric Device for Rapid and Sensitive Urinary Oxalate Determinations

A Cost Effective Immobilization of Horseradish Peroxidase Nanoparticles on to Easy-To-Prepare Activated Plasticized Polyvinyl-Chloride Vial and Its Application

A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization

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