Zusfahair Zusfahair
Department of Chemistry, Faculty of Mathematics and Natural Sciences, Universitas Jenderal Soedirman, Purwokerto

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Journal : Molekul: Jurnal Ilmiah Kimia

Development of Urea Biosensor Based on Immobilized Urease in Chitosan Cryogel Zusfahair Zusfahair; Dian Riana Ningsih; Elok Dwi Putri Lestari; Amin Fatoni
Molekul Vol 14, No 1 (2019)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (671.474 KB) | DOI: 10.20884/1.jm.2019.14.1.523

Abstract

The development of biosensors using biological components has an important role in detecting the disease early because it has good selectivity and accuracy. In this study, a biosensor which made is a urea biosensor, based on immobilization urease in chitosan using adsorption techniques, to measure urea levels by colorimetric analysis with bromothymol blue (BTB) as an indicator. The purpose of this study was to find out how to measure urea levels using biosensors based on urease immobilization in chitosan and find out the biosensor performance including optimum enzymatic reaction time, linearity, the limit of detection, repetition, and determination of disrupting compounds. The study began with the making of an immobilization supporting matrix using chitosan which was made in the form of cryogel through an ionic gelation process which adsorbs the urease enzyme. Cryogel urease catalyzes the hydrolysis of urea into NH4+ and CO2-. The reaction product was added with the BTB indicator, and the color change formed was measured using a spectrophotometer. The results showed that the performance of urea biosensors was good enough for urea level detection systems by producing enzymatic reaction times at 15 minutes, linearity at 0.9951, detection limit at 0.018 mM, not affected by the addition of 0.05 mM ascorbic acid and 0.4 mM uric acid. This urea biosensor can be used up to 5 repetitions.
Immobilization and Characterization of Bacillus Thuringiensis HCB6 Amylase in Calcium Alginate Matrix Zusfahair Zusfahair; Dian Riana Ningsih; Dwi Kartika; Amin Fatoni; Indah Permatawati
Molekul Vol 12, No 1 (2017)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (508.968 KB) | DOI: 10.20884/1.jm.2017.12.1.249

Abstract

Free enzyme in solution react with substrates to result in products which cannot be recovered for reuse. These problems can be overcome to a certain extent by the use of enzyme immobilization method. Immobilized enzymes are more robust and more resistant to condition changes. More importantly, the heterogeneous immobilized enzyme systems allow an easy recovery of both enzymes and products, multiple re-uses of enzymes, and continuous operation of enzymatic processes. Entrapment of enzymes in Ca-alginate is one of the simplest methods of immobilization. The aim of this research was to obtain the optimum condition of the making of immobilized amylase beads using a Ca-alginate bead and to determine its characteristics. The optimization of immobilized amylase beads includes variation of sodium alginates and variations of enzyme contact time with CaCl2. The characterization of immobilized amylase includes determination of optimum substrate concentration, optimum pH, and optimum incubation time as well as amylase stability test. Amylase activity was determined by using dinitro salicylic (DNS) method. The results showed that the optimum immobilized amylase obtained at alginate concentrations of 5% (w/v), contact time of 60 minutes and immobilization efficiency of 67.5%. Furthermore, immobilized amylase showed optimum substrate concentration of 1.5-2.5% (w/v), optimum pH of 6, an optimum incubation time of 20 minutes with the activity of 179.8 U/mL. The KM value for free amylase and immobilized amylases were 0.3 mM and 0.12 mM respectively. Vmax value for free amylase and immobilized amylases were 105.3 U/mL and 10.1 U/mL respectively. Immobilized Amylase can be used up to six times with the residual activity of 52.7%.