Publications by authors named "Kanchanmala Deshpande"

Background: Synthesis and modification of cost-effective sorbents for removing heavy metals from water resources is an area of significance. It had been reported that materials with biological origins, such as agricultural and animal waste, are excellent alternatives to conventional adsorbents due to their higher affinity, capacity and selectivity towards metal ions. These properties of biomaterials help to reduce or detoxify metal ions concentration in contaminated water to acceptable regulatory standards.

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There is a need for analytical methods capable of monitoring urea levels in urine for patients under clinical monitoring to appraise renal function. Herein, we present a practical method to quantify levels of urea in human urine samples using flow injection analysis-enzyme thermistor (FIA-ET) biosensor. The biosensor comprises a covalently immobilized enzyme urease (Jack bean) on aminated silica support, which selectively hydrolyzes the urea present in the sample.

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A simple, miniaturized microplate chemiluminescence assay for determination of methyl parathion (MP) was developed in 384-microwell plates. Zirconia (ZrO(2)) was added in microwell for adsorption of acetylcholinesterase (AChE). The developed assay is based on inhibition of AChE by MP.

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A highly sensitive and specific enzyme inhibition assay based on alcohol oxidase (AlOx) and horseradish peroxidase (HRP) for determination of mercury Hg(II) in water samples has been presented. This article describes the optimization and miniaturization of an enzymatic assay using a chemiluminescence reaction. The analytical performance and detection limit for determination of Hg(II) was optimized in 96 well plates and further extended to 384 well plates with a 10-fold reduction in assay volume.

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A rapid, high-sensitivity, chemiluminescence (CL) enzyme assay for the determination of organophosphate (OP) residues in milk is presented. The assay for quantification of OP residues in milk is based on the inhibition of enzyme butyrylcholinesterase (BuChE). BuChE was stabilized and preloaded in 384 well plates at 30 °C.

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