Abstract

This study aims to characterize the phosphate buffer and urease enzymes through UV-Vis and SEM-EDS absorbance spectra using tungsten as an indicator electrode. The method used is a potentiometric biosensor with urease enzyme immobilization technique for urea analyte. A small detection range of 10-5-10-4M has been studied with PVA-enzyme coated indicator electrodes coated with PVC-KTpClPB. On this basis, the researchers increased the detection range by analyzing glutaraldehyde (GA) mixed with PVA-enzyme and o-NPOE mixed with PVC-KTpClPB. The best results of GA mixed PVA-enzyme at GA2.9% UV-Visible analysis. The best results were PVA-enzyme coated indicator electrodes coated with GA coated again with PVC-KTpClPB-o-NPOE SEM-EDS analysis on PVA-enzyme samples 3x coated with GA 1x and PVC-KTpClPB-o-NPOE 1x with o-NPOE variation of 61% and 66%.

Highlights

  • Research has been carried out on indicator electrodes coated with PVA-enzyme coated with PVCKTpClPB with a detection range of 10-5-10-4 M (Hakim, 2019)

  • Characterization Results of SEM-EDS B1-4 and B3-4 The difference in the best results for indicator electrodes B1-4 and B3-4 was analyzed by variable signal analysis supported by SEM-EDS analysis in Table 1. that more weight percent, atomic percent and tungsten ratio on indicator electrode B3-4 than indicator electrode B1- 4

  • Based on the data above, the manufacture of tungsten indicator electrodes with the best membrane modifications at B1-4 and A1-4 66%

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Summary

Introduction

Research has been carried out on indicator electrodes coated with PVA-enzyme coated with PVCKTpClPB with a detection range of 10-5-10-4 M (Hakim, 2019). This electrode analysis has been characterized using SEM-EDS (Hakim, 2018). Range 5.10-7-10-2 M, according to (Rahman, 2008), on this basis the researchers increased the detection range with GA and o-NPOE. GA has been shown to be effective in increasing the strength and thermal stability of gelatin films (Lin, 2020). GA as a crosslinker enhances the properties of the ionogel, achieving a 5-fold higher activity than the free enzyme and for reuse at 70oC. The chemical composition and morphology were studied by electron

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