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Horseradish peroxidase (HRP) modified GRE was applied in cathode (HRP/GRE) of the same biofuel cell.
Only HRP modified with GO-GQDs offers an enhanced activity (more than 1.9 times of pristine enzyme) and thermo-stability.
Experiments were performed using horseradish peroxidase (HRP) modified nanopores with modified pore diameters (~34 nm) in 0.1 M KCl, buffered at pH 7.0 with 0.1 M PBS.
Two different modified Sepharose beads were used, IDA- and DEAE-Sepharose, for the immobilisation, respectively, of horseradish peroxidase (HRP) modified with histidine, and choline oxidase (Chx).
Meanwhile, the G-quadruplex/hemin/aptamer and horseradish peroxidase (HRP) modified gold nanoparticles (G-quadruplex/hemin/aptamer AuNPs HRP) nanoprobe was desiG-quadruplex/hemin/aptamer AuNPs HRP
The HRP modified with green luminescent GO-GQDs was also employed as a biocatalyst for sensing of H2O2 by a fluorometric sensor.
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A bi-enzyme biosensor, alcohol oxidase (AOX) and osmium-wired horseradish peroxidase (Os-HRP) modified carbon screen printed electrode (SPE), was designed for detection of methyl mercaptan in aqueous phase.
Meanwhile, the aggregated ABTS+ passed through the HRPs modified nanopores needed a −300 mV threshold voltage.
Here, the HRPs modified solid-state nanopore with diameter of ~34 nm is used as the hydrogen peroxide detection channel.
The aggregated cationic radical ABTS+ produced inside the solid-state nanopore and reduced the ionic current in the HRPs modified solid-state nanopore, are consistent with voltage-dependence.
However, the translocation events gradually disappeared when the biased voltage was kept below −300 mV, which suggested that aggregated ABTS+ across HRPs modified nanopores needed a −300 mV threshold voltage.
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