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All Journal Indonesian Journal of Chemistry Indonesian Chimica Letters
Andriana Kusuma Pertiwi
Department Of Chemistry, Faculty Of Mathematics And Natural Sciences, Brawijaya University, Jl. Veteran, Malang 65145, Indonesia
Chemical Engineering, Chemistry & Bioengineering Chemistry

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Microencapsulation of Ruellia tuberosa L. Extracts Using Alginate: Preparation, Biological Activities, and Release Andriana Kusuma Pertiwi; Choirin Annisa; Zubaidah Ningsih; Anna Safitri
Indonesian Journal of Chemistry Vol 23, No 2 (2023)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijc.76821

Abstract

The bioactive compounds naturally present in plants have great importance due to their biological characteristics. These substances could lose their active characteristics since they are highly unstable. Microencapsulation is one of the techniques to improve stability and protect these compounds. In this work, Ruellia tuberosa L. ethanolic extracts microcapsules were prepared using a freeze-drying method by varying pH, alginate concentration, and stirring time. The encapsulation efficiency (EE), characteristics, alpha-amylase inhibition activity, and release behavior of the microcapsules were investigated. The results highlighted that the highest encapsulation efficiency for the microcapsules was obtained at pH 6, alginate concentration of 1% (w/v), and 30 min of stirring time (51.63% EE). The microcapsules mostly had spherical shapes with a mean diameter of 197.53 μm. The alpha-amylase inhibition assay from microcapsules resulted in the IC50 value of 46.66 ± 0.13 μg/mL, demonstrating high biological activity. The bioactive substances from microcapsules were released during intervals of 30–120 min at pH values of 1.2 and 7.4. Only 3.51% of the bioactive substances were released at pH 1.2 after 120 min, compared to 55.78% at pH 7.4. Overall, this work confirms the possibility of developing plant extracts with preserved biological activity using the produced microcapsules.
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.
Strategic Optimization of Fractionation and Dialysis Buffer pH to Enhance Goat Liver-Uricase Activity Zain, Romzi Al Amiri; Handayani, Wuryanti; Sjaifullah, Achmad; Pertiwi, Andriana Kusuma; Ratnadewi, Anak Agung Istri; Sudarko, Sudarko
Indonesian Chimica Letters Vol. 5 No. 1 (2026)
Publisher : Department of Chemistry, FMIPA, UNEJ

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.19184/icl.v5i1.60008

Abstract

Uricase is an important enzyme that catalyzes the oxidation of uric acid to allantoin and has potential applications in clinical diagnostics and biotechnology. However, its activity and stability are greatly influenced by purification conditions. This study aimed to optimize ammonium sulfate fractionation and the pH of the dialysis solution to enhance the activity of uricase isolated from goat liver. The enzyme was extracted and subjected to stepwise ammonium sulfate precipitation at different saturation levels, followed by dialysis using buffers with varying pH values. Enzyme activity and protein concentration were determined to calculate specific activity, and SDS–PAGE analysis was performed to evaluate the purification profile. The results showed that the optimal ammonium sulfate fraction for uricase precipitation was 0–20% saturation, yielding the highest specific activity of 0.0034 ± 0.001 U/mg. Further dialysis optimization indicated that a pH of 8.5 was the most favorable condition, yielding the highest enzyme activity of 0.0038 ± 0.001 U/mg. SDS–PAGE analysis showed reduced contaminant protein bands after purification, indicating improved enzyme purity. These findings suggest that precise control of salt concentration and buffer pH is crucial for maintaining uricase stability and enhancing its catalytic performance. Overall, the combination of optimized ammonium sulfate fractionation and dialysis conditions effectively improved the purity and activity of uricase, providing a useful basis for further development and application of this enzyme in biochemical and industrial processes.
Co-Authors Achmad Sjaifullah Anak Agung Istri Ratnadewi Anna Safitri Choirin Annisa Febriani, Nurul Afifah Sudarko Sudarko Sudarko Wuryanti Handayani Zain, Romzi Al Amiri Zubaidah Ningsih