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All Journal VALENSI JURNAL KIMIA SAINS DAN APLIKASI Jurnal Natur Indonesia The Journal of Pure and Applied Chemistry Research Jurnal Kimia Riset ALCHEMY Jurnal Penelitian Kimia Molekul: Jurnal Ilmiah Kimia Dinamika Journal : Pengabdian Masyarakat Jurnal Serambi Abdimas Jurnal Natural Darma Sabha Cendekia Molekul: Jurnal Ilmiah Kimia
Zusfahair Zusfahair
Jurusan Kimia Fakultas MIPA Universitas Jenderal Soedirman Purwokerto
Agriculture, Biological Sciences & Forestry Humanities Astronomy Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Earth & Planetary Sciences Economics, Econometrics & Finance Energy Engineering Environmental Science Immunology & microbiology Languange, Linguistic, Communication & Media Materials Science & Nanotechnology Medicine & Pharmacology Neuroscience Physics Other

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Immobilization of urease from Phaseolus vulgaris L. seeds using calcium alginate as a support matrix ZUSFAHAIR ZUSFAHAIR; DIAN RIANA NINGSIH; AMIN FATONI; ELY SETIAWAN
Jurnal Natural Volume 22 Number 3, October 2022
Publisher : Universitas Syiah Kuala

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.24815/jn.v22i3.26056

Abstract

Urease is an enzyme that functions as a catalyst in the hydrolysis of urea into ammonia and carbon dioxide. The industrial sector has made extensive use of urease. To date, enzymes are used in free form, deemed less effective. Therefore, enzymes are used in immobilized form because they can be utilized repeatedly. This research aimed to isolate urease from kidney bean (Phaseolus vulgaris L.) seed and immobilize it using a Ca-alginate support matrix and a trapping technique. Eight days were devoted to germinating kidney bean seeds to begin the investigation. Isolation of crude urease extract from kidney beans was carried out using phosphate buffer pH 7. It was then immobilized with Ca-alginate at different concentrations of Na-alginate and contact times The crude free and immobilized urease extract was further characterized including pH, temperature and stability of repeated use. The urease activity was determined using the Nessler method using a spectrophotometer. The results demonstrated that urease immobilization from kidney bean seeds with a Ca-alginate matrix was most effective at a concentration of 5% Na-alginate and a contact period of 60 minutes, yielding a value of 5.92 U/mL. The optimal pH of free and immobilized urease was 7 and 8, respectively, and temperatures of 35 and 40 °C, respectively. The immobilization of urease from kidney bean seeds using a Ca-alginate support matrix increased the stability of recurrent use by fivefold, while the relative urease activity remained at 52%.
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%.
Immobilization of Urease from Psophocarpus tetragonolobus L. DC. using Natrium Alginate Supporting Matrix Zusfahair, Zusfahair; Ningsih, Dian Riana; Lestari, Puji; Bilalodin, Bilalodin; Aryanti, Eva; Muslihah, Niken Istikhari
Molekul Vol 19 No 1 (2024)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20884/1.jm.2024.19.1.7335

Abstract

Urease is an enzyme that has the role to hydrolyzes urea into ammonia and carbon dioxide. Immobilization is one of the most efficient strategies to improve its activity recovery and properties of urease. This research started with the germination of winged beans for 8 days. The winged bean was extracted by grinding using a mortar and pestle and then added with phosphate buffer at pH 7. The solution was homogenized using a stirrer and then centrifuged in cold conditions so that an extract of urease was obtained. Urease extracts were immobilized using a chitosan-supporting matrix. Optimization of the immobilization process of urease extract includes the concentration of chitosan and sodium tripolyphosphate (TPP) and contact time. The obtained was free and immobilized urease activities then tested using the Nessler method and measured using a UV-Vis spectrophotometer with a wavelength of 500 nm. The obtained data were then statistically tested using ANOVA. Urease-chitosan beads were further tested in repeated use and analyzed with SEM-EDX (Scanning Electron Microscopy-Energy Dispersive X-ray). The results showed that the optimum conditions for making urease-chitosan beads were a concentration of 4% (w/v), 2.5% (w/v) TPP, and 60 minutes of contact time, resulting in an activity value of 15.076 U/mL, which can be used 5 times with 46% activity from the initial activity. The EDX analysis results after the addition of the enzyme showed atom composition changes leading to increasing carbon and nitrogen contents. The existence of phosphor showed that TPP was a chitosan cross-link compound. Keywords: Chitosan, immobilization, TPP, urease, winged bean
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 Nurdin AMIN FATONI Anung Riapanitra Apriliadina, Inessa Putri Ari Asnani Aryanti, Eva Bilalodin Bilalodin Dadan Hermawan 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 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 Diyu Mantari Dwi Kartika Elok Dwi Putri Lestari ELY SETIAWAN Fajar Nuradha Febrina Nur Habibah Indah Permatawati Irmanto Irmanto Istinganatun Khoeriyah Luthfia, Adilla Mardiyah Kurniasih Mardiyah Kurniasih Mei Lianasari Mekar Dwi Anggraeni Muslihah, Niken Istikhari Niken Istikhari Muslihah Nuraini, Aprilia Nafi Puji Lestari PUJI LESTARI Puji Lestari Puji Lestari Purwati Purwati Purwati Purwati Purwati Purwati Purwati Purwati Purwati Purwati Senny Widyaningsih Senny Widyaningsih Senny Widyaningsih Setiawan, Ely Sulistyowati, Aris Suyata Suyata Tien Setyaningtyas Uyi Sulaeman Vika Aprilia Puspitarini