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Anak Agung Istri Ratnadewi
Department Of Chemistry, Faculty Of Mathematics And Natural Sciences, University Of Jember
Agriculture, Biological Sciences & Forestry Humanities Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Civil Engineering, Building, Construction & Architecture Computer Science & IT Control & Systems Engineering Education Electrical & Electronics Engineering Engineering Immunology & microbiology Industrial & Manufacturing Engineering Mathematics Mechanical Engineering Physics Other

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Purification of Xylooligosaccharide From Casavva Pulp by Ultrafiltration Method Ratnadewi, Anak Agung Istri; Fauziyah, Kamelia Rizqi; Indarti, Dwi
BERKALA SAINSTEK Vol 9 No 2 (2021)
Publisher : Universitas Jember

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.19184/bst.v9i2.23388

Abstract

Xylan is the main component of hemicellulose. Xylan can be extracted from agricultural waste, such as cassava pulp. Xylan is used as an endo-β-1,4-D-xylanase substrate to produce impure xylooligosaccharides (XOS)This study aims to purify XOS from cassava pulp using the ultrafiltration method. The components of XOS obtained from the enzymatic hydrolysis were analyzed using thin layer chromatography (TLC) and densitometry methods. In addition, the XOS was purified by the ultrafiltration method using a cellulose membrane with a Molecular Weight Cut Off (MWCO) of 12 kDa. The permeate obtained from the purification results was also analyzed using TLC and densitometry. The results of this study indicated that the components in XOS cassava pulp before and after purification by the TLC method were X5 and X6, while the XOS components before and after purification by the densitometric method were X3, X4 and X5.
The Effect of Substrate Concentration and Incubation Time on The Activity of The Uricase Enzyme From Goat Liver Handayani, Wuryanti; Febriani, Nurul Afifah; Ratnadewi, Anak Agung Istri; Sudarko; Pertiwi, Andriana Kusuma
Indonesian Chimica Letters Vol. 3 No. 2 (2024)
Publisher : Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Jember

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.19184/icl.v3i2.4255

Abstract

Uricase is an oxidoreductase enzyme that catalyzes the degradation of uric acid into allantoin, hydrogen peroxide, and carbon dioxide. Allantoin, the primary product of uric acid degradation, exhibits 5-10 times greater solubility in water compared to uric acid. This property underscores the importance of uricase in managing hyperuricemia, a condition characterized by elevated uric acid levels in the blood. Hyperuricemia is associated with diseases such as gout, kidney dysfunction, and hypertension. While humans and primates lack the uricase enzyme, it is naturally present in the liver of non-primate mammals, including goats. This study investigated the activity of uricase extracted from goat liver, focusing on the optimum concentration of uric acid as the substrate and incubation time necessary for achieving maximum enzymatic activity. Goat liver samples were processed using borate buffer (pH 8.5) ammonium sulfate fractionation and dialysis to isolate uricase. The enzymatic activity was evaluated at uric acid concentrations of 1.0, 1.5, 2.0, 2.5, and 3.0 mM and incubation times of 3.0, 3.5, 4.0, 4.5, 5.0, 5.5, and 6.0 hours. The results revealed that the optimum substrate concentration for uricase was 2 mM, yielding total enzyme activity of 0.6704 U/mL and specific activity of 0.0443 U/mg. Additionally, the optimum incubation time was determined to be 5 hours, resulting in total enzyme activity of 0.8421 U/mL and specific activity of 0.0556 U/mg. These findings provide valuable insights into enhancing uricase activity and optimizing its application in therapeutic strategies for hyperuricemia management. Further research is recommended to explore the potential of uricase in clinical and pharmaceutical contexts.
Isolation and Characterization of Uricase Produced from Chicken Liver Wuryanti Handayani; Nasrul Amaliyatun Naja; Muhamad Kiki Afindia Joenata; Ratnadewi, Anak Agung Istri
Journal of Bio-Molecule Research and Engineering Vol 1 No 1 (2022)
Publisher : Universitas Airlangga

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20473/jbiome.v1i1.35859

Abstract

Uricase is an enzyme that degrades uric acid into allantoin. One of the uricase sources is obtained from chicken species (Gallus gallus domesticus) liver which are broiler and native chicken. This study aims to determine the maximum uricase activity in broiler and native chicken liver. The uricase activity was obtained by measuring the uric acid concentration as uricase substrate using spectrophotometric method and wavelength at 291 nm. Uricase isolation was carried out into extraction process, ammonium sulfate fractionation (0-60% saturation of ammonium sulfate), and dialysis. During isolation process, centrifugation speed was also optimized to obtain the maximum uricase crude extract and uricase activity. The molecular weight of uricase was also determined by SDS PAGE. The result showed that the highest uricase activity remained using centrifugation speed of 15,000 rpm. The optimum uricase fraction for broiler chicken liver was obtained at 20-40% saturation of ammonium sulfate with uricase activity was 1.854 x 10-2 U/mg, and the uricase fraction for native chicken liver was obtained at 40-60% saturation of ammonium sulfate with uricase activity was 2.496 x 10-2 U/mg. The optimum fraction for uricase production and isolation is carried out to the dialysis process. The optimum uricase activity of broiler chicken liver crude extract was 4.921 x 10-4 U/mg, the uricase fraction was 3.989 x 10-3 U/mg, and the dialysate was 5.120 x 10-3 U/mg. While the native chicken liver crude extract was 2.980 x 10-4 U/mg, the uricase fraction was1.415 x 10-2 U/mg, and the dialysate was 1.753 x 10-2 U/mg. The molecular weight of the uricase was around 35 kDA according to the SDS PAGE result.
Immobilization of Endo-Β-1,4-D-Xylanase using Alginate/Nanocellulose for Xylooligosaccharide Production Ratnadewi, Anak Agung Istri; Aprilia, Selvina Rizky; Piluharto, Bambang; Yulvia, Ana
Indonesian Chimica Letters Vol. 2 No. 2 (2023)
Publisher : Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Jember

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.19184/icl.v2i2.5607

Abstract

Free endo-β-1,4-D-xylanase cannot be used more than once, so it needs to be modified by immobilizing the enzyme. Endo-β-1,4-D-xylanase was obtained from termite abdomen sources by isolation, ammonium sulfate purification, and dialysis methods. Endo-β-1,4-D-xylanase was immobilized with an alginate/nanocellulose matrix. This study aims to determine the activity, protein content, and repeated use of immobilized Endo-β-1,4-D-xylanase. This study used variations of Alginate/nanocellulose (0; 2.5; 5; 7.5; 10) %. Protein levels of Endo-β-1,4-D-xylanase were tested using the Bradford method and activity using the Miller method. The total protein bound to the immobilized Endo-β-1,4-D-xylanase was stated with the immobilized yield data. The immobilized yield with the composition of Alginate Nanocellulose (ANC) (0%) was 45.33% greater than the other compositions. Immobilized Endo-β-1,4-D-xylanase activity is efficient. ANC 5% produces an efficiency of 62.384% at the 12th hour, which is greater than the other ANC compositions.
Co-Authors Agung Budi Santoso Andika Ade Kurniawan Andika Ade Kurniawan, Andika Ade Andriana Kusuma Pertiwi Aprilia, Selvina Rizky Arianti, Fefpi Nur Afnifitri Wias Asnawati Bambang Piluharto Dwi Indarti Eka Yuni Kurniawati Eka Yuni Kurniawati, Eka Yuni Fauziyah, Kamelia Rizqi Febriani, Nurul Afifah Firda Marta Safitri Hefinda Erfiandika Indras Dwi Anggita Jayus, Jay Kristiyono, Rimba Candra Muhamad Kiki Afindia Joenata Nasrul Amaliyatun Naja Nasution, Annio Indah Lestari Nurhayati Nurhayati Nyoman Gede Krishnabudi Rosa Safitri Selvi Marcellia Siti Nur Avida Sudarko Sudarko Sudarko Wuryanti Handayani Yulvia, Ana