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KARAKTERISASI ENZIM AMILASE DARI BAKTERI Bacillus amyloliquefaciens Ningsih, Dian Riana; Rastuti, Undri; Kamaludin, Ridlwan
Prosiding Vol 3, No 1 (2012)
Publisher : Prosiding

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Abstract

Enzim Amilase merupakan salah satu jenis enzim yang berperan penting dalam industri. Enzim amilase digunakan untuk menghidrolisis pati menjadi molekul karbohidrat yang lebih sederhana, yaitu dekstrin, maltosa dan glukosa. Industri yang menggunakan amilase antara lain: dalam industri kertas, industry detergen, industry tekstil, industry obat dan industri roti dan kue. Bacillus amyloliquefacien merupakan salah satu bakteri yang dapat menghasilkan amilase. Tujuan dari penelitian ini adalah menentukan aktivitas enzim amylase dan mengkarakterisasi sifat biokimia enzim amylase dari B. amyloliquefaciens. Tahapan penelitian ini adalah penentuan waktu produksi optimum enzim amylase, produksi amylase dan penentuan aktivitas enzim amylase pada berbagai suhu dan pH. Penentuan aktivitas amylase menggunakan metode Nelson Somogyi. Hasil penelitian menunjukkan bahwa enzim amylase yang dihasilkan oleh B. amyloliquefaciens mempunyai waktu produksi optimum pada jam ke 24 (1.4986 U/ml), temperature optimum 30-60 oC dan pH optimum 6-7.
Hidrolisis Pati Ganyong (Canna edulis) dengan Amilase Bakteri Flavobacterium sp. PTBT I untuk Produksi Bioetanol Ningsih, Dian Riana; Zusfahair, Zusfahair; Fatoni, Amin
Jurnal Natur Indonesia Vol 15, No 2 (2013)
Publisher : Lembaga Penelitian dan Pengabdian kepada Masyarakat Universitas Riau

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (205.385 KB) | DOI: 10.31258/jnat.15.2.92-98

Abstract

Bioethanol is an alternative energy of fuels produced from vegetable materials. Vegetable materials that can be used as rawmaterial for bioethanol is ganyong because it contains 22.60 g starch in 100 g ganyong. The production of bioethanol fromstarch material consisted of two steps, hydrolysis and fermentation. One of the steps to increase the value of bioethanolfrom starch of ganyong was hydrolysis process using thermostable amylase enzyme isolated from Flavoacterium sp.PTBT I bacteria was isolated from hot spring of Pancuran Tujuh Baturraden. The aim of this research was to use thermostableamylase to hydrolyze starch of ganyong and glucose produced to result bioethanol. The result of this research showed thatthe optimum condition hydrolysis starch of ganyong was using thermostable amylase acquired at substrate concentrationof 3% (b/v), and incubation time of about 75 minutes. The value of bioethanol increased with time of fermentation, from thefirst to fourth day, which was 0.8361; 2.2379; 5.7590 and 10.5787% (v/v), respectively.
Determination of Cu and Pb concentrations based on urease activity inhibition of Durio zibethinus L. seeds Zusfahair, Zusfahair; Fatoni, Amin; Ningsih, Dian Riana; Riapanitra, Anung
Molekul Vol 16, No 2 (2021)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (217.71 KB) | DOI: 10.20884/1.jm.2021.16.2.736

Abstract

The determination of heavy metal concentrations has been carried out using sophisticated instruments, and therefore a simple and reliable alternative method is needed as a comparison. The study aimed to determine Cu and Pb concentration of standard solution using the urease activity inhibition method of Durio zibethinus L.  seeds.  The research started with urease extraction from Durio D. zibethinus L. seeds. The activity of the obtained extract was determined using the Nessler method. The optimum substrate concentration was also determined. Urease activity inhibition was carried out using various metal solution concentrations, which continued by plotting a log graph of urea concentration vs. %inhibition. The obtained graph would then determine the metal concentration in a synthetic water sample. The data was then compared to the measurement, determined by the Atomic Absorption Spectrophotometry (AAS) method. Results of the study showed that the urease activity of D. zibethinus L.seeds was 296.774 U/mL. Urease activity was optimum at a urea concentration of 0.3 M. The comparison Cu, and Pb concentration determination using the urease inhibitory activity and AAS methods showed no significant difference at 95% confidence level. This research showed that urease of D. zibethinus L. seed could be used to determine Cu and Pb's concentration based on its inhibiting activity.
Ointment Formulation of Arumanis Mango (Mangifera indica L.) Leaf Extract with Chitosan Tripoliphosphate Matrix as Antibacterial Dian Riana Ningsih; Anung Riapanitra; Zusfahair Zusfahair; Uyi Sulaeman; Istinganatun Khoeriyah
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.2023.18.1.5725

Abstract

This report presented the synthesis of Arumanis mango (Mangifera indica L.) leaf extract with chitosan tripolyphosphate matrix and its antibacterial activity. This research aimed to obtain an ointment formulation from mango leaf extract with chitosan tripolyphosphate matrix, to figure out the characteristics, including the particle morphology, and to determine the optimum formulation and the characterization of the antibacterial ointment. The research showed that extract morphology with chitosan tripolyphosphate was uneven-edge aggregates. Antibacterial tests were conducted on P. acnes and E. coli bacteria. The formula giving the greatest antibacterial activity was further utilized for the ointment preparations and then was characterized for 16 days. Formula C (chitosan and NaTPP 1: 0.0992(%)) gave the most excellent inhibition zone for P. acnes and E. Coli bacteria, at 7.94 mm and 10.02 mm, respectively. The obtained ointment preparation was white color homogeneous semi-solid with protective properties. The spreading power of the ointment was 5.25 – 6.25 cm, with the adhesive power of 1 – 5 seconds and pH of 6.0 – 6.4. The ointment's antibacterial activity was tested against P. acnes and E. coli bacteria using the formation of inhibition zone method. The activity of ointment prepared on day one against P. acnes and E. coli was at 14.03 mm and 14.24 mm, respectively, while the activity on day 16 against P. acnes and E. coli was at 9.33 mm and 9.98 mm, respectively.
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