Andriana Kusuma Pertiwi
Department Of Chemistry, Faculty Of Mathematics And Natural Sciences, Brawijaya University, Jl. Veteran, Malang 65145, Indonesia

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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.