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All Journal HAYATI Journal of Biosciences VALENSI Jurnal Natur Indonesia Jurnal Kimia Riset Jurnal Zarah Science and Technology Indonesia Jurnal Farmasi Sains dan Komunitas ALCHEMY Jurnal Penelitian Kimia Molekul: Jurnal Ilmiah Kimia SAP (Susunan Artikel Pendidikan) JURNAL LENTERA BISNIS Jurnal Natural Darma Sabha Cendekia Molekul: Jurnal Ilmiah Kimia
AMIN FATONI
Department Of Chemistry, Faculty Of Mathematics And Natural Sciences, Universitas Jenderal Soedirman, Purwokerto, Indonesia
Agriculture, Biological Sciences & Forestry Astronomy Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Earth & Planetary Sciences Economics, Econometrics & Finance Education Energy Environmental Science Immunology & microbiology Materials Science & Nanotechnology Medicine & Pharmacology Neuroscience Physics Social Sciences

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Journal : Molekul: Jurnal Ilmiah Kimia

 1 
Chiral Separation of Econazole by High Performance Liquid Chromatography Method using Cyclodextrin as Chiral Column Dadan Hermawan; Cacu Cacu; Khansa Salsabila; Suwandri Suwandri; Amin Fatoni; Uyi Sulaeman; Ponco Iswanto; Mudasir Mudasir; Hassan Y. Aboul-Enein
Molekul Vol 17 No 2 (2022)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20884/1.jm.2022.17.2.6348

Abstract

The chiral separation of econazole, an antifungal drug with one chiral center has been successfully carried out using the high-performance liquid chromatography (HPLC) method. Enantioresolution of econazole (Rs = 2.29) was achieved using cyclodextrin-based chiral column (Astec Cyclobond, 25 cm × 4.6 mm × 5 μm), mobile phase composition of acetonitrile : water (0.2% HCOOH) (20:80, v/v), and UV detection of 220 nm.The optimized HPLC method has been applied for the quantitative determination of econazole in the pharmaceutical (liquid) sample withpercentage recovery of 100.75 % (RSD = 0,95%; n = 3). The effect of several HPLC parameters on the chiral separation of econazole was also evaluated and the method was successfully validated in terms of linearity, accuracy, precision, and selectivity. The present HPLC method was simple, short analysis time, and high resolution.
The Isolation, Immobilization, and Characterization of Urease from The Seeds of Winged Bean (Psophocarpus tetragonolobus (L.) DC. Zusfahair, Zusfahair; Ningsih, Dian Riana; Fatoni, Amin; Bilalodin, Bilalodin; Nuraini, Aprilia Nafi
Molekul Vol 18 No 1 (2023)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20884/1.jm.2023.18.1.5932

Abstract

Urease has been utilized in the field of health and industry. Urease is commonly used in the form of free enzyme, so that the utilization is limited. Urease efficiency can be improved using immobilization enzyme. This research aimed to do the urease isolation, immobilization, and characterization from the winged bean seeds. This research was started by determining the amino-acid content of winged bean seeds using the Liquid chromatography-mass spectrometry (LCMS). The winged bean seeds were germinated and extracted. The obtained crude extract’s activity was determined using Nessler reagent and measured using UV-Vis spectrophotometer with the wavelength of 500 nm. The urease of winged bean seeds was immobilized using the alginate matrix. The optimization of urease-immobilized beads could be made through the variations of natrium alginate concentration and beads formation periods in solution CaCl2. Characterization free and immobilized urease were made using the variations of urea substrate concentration, pH, temperature, and also the repeated utilization of immobilized urease. Winged bean seeds are rich with essential amino acid, such as leucine, isoleucine, histidine, phenylalanine, and valine. The urease obtained from the winged bean seeds had the optimum activity in the germination period of 8 days. The urease immobilization showed the optimum condition in the natrium alginate concentration of 5% (w/v) and beads formation period in solution CaCl2 for 60 minutes. The characterization results of free urease and immobilization had the optimum condition at the urea substrate of 0.2 M, and pH 7. Free urease had the optimum temperature of 35 oC, while the immobilized urease had the optimum temperature of 40 oC. The immobilized urease had the utilization stability up to 5 times with the relative activity of 48%. The EDX analysis results showed that the alginate did not contain N, while alginate urease beads contained N as much as 12%.
Optimization and Characterization of Urease Immobilization from Red Lentil Seeds (Lens culinaris) Using Chitosan zusfahair, zusfahair; Ningsih, Dian Riana; Bilalodin, Bilalodin; Fatoni, Amin; Luthfia, Adilla; Purwati, Purwati; Muslihah, Niken Istikhari; Apriliadina, Inessa Putri
Molekul Vol 20 No 2 (2025)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20884/1.jm.2025.20.2.13134

Abstract

ABSTRACT. Urease is an enzyme that plays a vital role in catalyzing the hydrolysis of urea into ammonia (NH3) and carbon dioxide (CO2). This study focuses on the isolation of urease from red lentil seeds, followed by its immobilization. The objective of this research is to optimize and characterize urease that has been immobilized using chitosan and activated with glutaraldehyde. Red lentil seeds were processed with a mortar and pestle at low temperatures (4 °C) to obtain a crude enzyme extract, which was then concentrated using 50% acetone (P50) prior to immobilization. The optimization process for P50 urease immobilization involved assessing various factors, including chitosan concentration, glutaraldehyde concentration, temperature, and the immersion duration in glutaraldehyde. The findings revealed that the optimal conditions for immobilizing P50 urease were achieved at a chitosan concentration of 0.75%, with a 2% glutaraldehyde soak at 25 °C for 2 hours, resulting in an enzyme activity of 7.042 U/g. The immobilized P50 urease demonstrated the ability to be reused up to 7 times while maintaining 51% of its initial activity. Scanning Electron Microscopy (SEM) analysis indicated morphological changes in the beads after the addition of glutaraldehyde and the enzyme, shifting from a rounded to an irregular shape. Additionally, Fourier Transform Infrared Spectroscopy (FTIR) analysis identified C-N and C=N peaks, confirming the successful incorporation of glutaraldehyde. Keywords: immobilization, red lentil seeds, glutaraldehyde, chitosan, urease
Partial Purification and Characterization of Urease from Red Lentils (Vicia lens (L.) Coss. & Germ.) Zusfahair, Zusfahair; Ningsih, Dian Riana; Bilalodin, Bilalodin; Fatoni, Amin; Setiawan, Ely; Sulistyowati, Aris
Molekul Vol 20 No 1 (2025)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20884/1.jm.2025.20.1.12920

Abstract

ABSTRACT. Urease is an enzyme that catalyzes the hydrolysis of urea into ammonia and carbon dioxide. A significant application of urease is found primarily in food, medical equipment and biosensor industries. This research aims to analyze the amino acid content of red lentil seeds and the extraction, purification, and characterization of urease from red lentils. The study started by analyzing the amino acid content in red lentil seeds using High-Performance Liquid Chromatography (HPLC). The red lentil seeds were extracted using phosphate buffer pH 7.0 and separated using centrifugal separation technique until crude extract of urease was produced. The crude extract of urease was then concentrated using acetone at varied saturation level (33, 41, 50, 60, and 67%). The fraction with the highest specific activity was then analyzed using SDS-PAGE method and characterized for its pH, incubation temperature, and substrate concentration against the urease activity. The urease activity was determined using Nessler method. The research results showed that red lentils seeds contained all essential amino acids. The highest specific activity was found in the fraction at 50% acetone saturation level (F50) and purity level 6.3 times than the crude extract. The characterization result indicated that F50 was purer than the crude extract. The optimum urease activity of crude extract and F50 was obtained at pH 7.0 and an incubation temperature of 35 °C. The KM value of F50 was lower than crude extract. F50 has a higher affinity for binding to substrates so that the enzyme has higher efficiency in forming the products. Urease from red lentil seeds concentrated using acetone was 50% more potent as a catalyst than the crude extract. The research data will be the basis for the application of this urease. Keywords: Acetone, characterization, partial purification, red lentil, urease
Co-Authors A.A. Ketut Agung Cahyawan W Ahmad Aminudin AHMAD ENDANG ZAINAL HASAN Ahmad Mudzakir Anung Riapanitra Apriliadina, Inessa Putri Ari Asnani Bilalodin Bilalodin Cacu Cacu Dadan Hermawan Dadan Hermawan Dadan Hermawan Dadan Hermawan, Dadan Darul Santri Pertiwi Dian Riana Ningsih DIAN RIANA NINGSIH Dian Riana Ningsih Dian Riana Ningsih Dian Riana Ningsih Dian Riana Ningsih Dian Riana Ningsih Dian Riana Ningsih Dian Riana Ningsih Dwi Agustina V Dwi Kartika Elok Dwi Putri Lestari ELY SETIAWAN Hartiwi Diastuti Hassan Y. Aboul-Enein HENDRI WASITO I MADE ARTIKA Indah Permatawati Khansa Salsabila Luthfia, Adilla Mala Nurilmala Mando Hastuti Mardiyah Kurniasih Mekar Dwi Anggraeni Mekar Dwi Anggraeni Mekar Dwi Anggraeni Mudasir Mudasir Muslihah, Niken Istikhari Nina Adriani Nuraini, Aprilia Nafi Ponco Iswanto Purwati Purwati Setiawan, Ely Sulistyowati, Aris Suwandri Suwandri Suwandri Suwandri Suyata Suyata Tien Setyaningtyas Uyi Sulaeman Vika Aprilia Puspitarini Vonia Febriana Hidayah Warsinah Warsinah Yulia Yulia Yulita, Inelda Zusfahair Zusfahair