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All Journal Jurnal Ilmiah Arena Tekstil Acta Biochimica Indonesiana JKPK (Jurnal Kimia dan Pendidikan Kimia) Journal of Multidisciplinary Applied Natural Science
IHSANAWATI IHSANAWATI
Kelompok Keahlian Biokimia FMIPA – ITB Jl Ganesha No. 10, Bandung
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Energy Environmental Science Immunology & microbiology Industrial & Manufacturing Engineering Materials Science & Nanotechnology Mathematics Physics

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ISOLASI DAN KARAKTERISASI BAKTERI PENGHASIL ENZIM LIPASE EKSTRASELULERDARI LUMPUR AKTIF INSTALASI PENGOLAHAN AIR LIMBAH INDUSTRI TEKSTIL Kasipah, Cica; Rismayani, Sinta; Ihsanawati, Ihsanawati; Nurachman, Zeily
Arena Tekstil Vol 28, No 1 (2013)
Publisher : Arena Tekstil

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (3387.131 KB)

Abstract

Lumpur aktif dari instalasi pengolahan air limbah industri tekstil mengandung berbagai jenis mikroorganisme antara lain mikroorganisme yang memiliki aktivitas lipase yang tinggi. Tujuan penelitian ini adalah mengisolasi dan mengkarakterisasi bakteri penghasil enzim lipase ekstraseluler dari lumpur aktif instalasi pengolahan air limbah industri tekstil. Tahapan penelitian yang dilakukan meliputi isolasi bakteri penghasil enzim lipase ekstraseluler dari lumpur aktif melalui skrining dengan media yang mengandung rodamin dan minyak zaitun, penentuan aktivitas enzim lipase dan karakterisasi lipase yang dihasilkan terhadap variasi temperatur, pH, dan pengaruh ion Ca2+. Hasil identifikasi secara mikrobiologi menunjukkan bahwa bakteri penghasil enzim lipase ekstraseluler dari lumpur aktif adalah spesies Erwiniachrysantemi. Enzim lipase ekstraseluler tersebut memiliki aktivitas 4,75 U/mL dengan temperatur optimum 40oC dan pH optimum 9. Penambahan ion Ca2+ tidak memberikan pengaruh berarti terhadap aktivitas enzim lipase.
Optimization of Nitration of 3-Hydroxypyrazine-2-Carboxamide to 3-Hydroxy-6-Nitropyrazine-2-Carboxamide Setyowati, Widiastuti Agustina Eko; Ihsanawati, Ihsanawati; Alni, Anita
JKPK (Jurnal Kimia dan Pendidikan Kimia) Vol 8, No 3 (2023): JKPK (Jurnal Kimia dan Pendidikan Kimia)
Publisher : Program Studi Pendidikan Kimia FKIP Universitas Sebelas Maret

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20961/jkpk.v8i3.81987

Abstract

This study focuses on optimizing the synthesis of 3-hydroxy-6-nitropyrazine-2-carboxamide, a critical intermediate in producing various pyrazine-based pharmaceuticals. The compound is synthesized through the nitration of 3-hydroxypyrazine-2-carboxamide, employing sulfuric acid (H2SO4) and potassium nitrate (KNO3) as reagents. The research aimed to refine the synthesis process to enhance yield purity for pharmaceutical applications. The optimization entailed adjusting the reagents' composition and solvents, specifically the ratio of substrate to KNO3, the volume of H2SO4 used per gram of substrate, and the temperatures for both the reaction and product precipitation. Optimal results were observed at a substrate-to-KNO3 ratio of 1:2, with 12 mL of H2SO4 per gram of substrate. The reaction temperature was set at 50°, and precipitation occurred effectively at 0°C. This optimized method significantly improved the yield and purity of the compound. The process demonstrated excellent repeatability, with yields ranging from 77% to 80%, a considerable increase from the 48% yield reported in previous studies. The molecular structure of the synthesized compound was confirmed through comprehensive spectroscopic analyses, including 1H NMR, 13C NMR, and High-Resolution Electrospray Ionization Time-of-Flight Mass Spectrometry (HRESI-TOF-MS). This research represents a significant advancement in synthesizing 3-hydroxy-6-nitropyrazine-2-carboxamide, offering a more efficient and reliable method for producing this key pharmaceutical intermediate. The improved synthesis process ensures higher yields and maintains the purity required for pharmaceutical applications, thereby contributing to the efficient development of pyrazine-based drug compounds.
Expression of Recombinant Plasmodium falciparum Cysteine-rich Protective Antigen (PfCyRPA) Fragment 26–181 in Escherichia coli BL21 CodonPlus (DE3) RIPL Masduki, Fifi Fitriyah; Prameswari, Aurelia Galih; Puspasari, Fernita; Ihsanawati, Ihsanawati; Natalia, Dessy
Acta Biochimica Indonesiana Vol. 8 No. 1 (2025): Acta Biochimica Indonesiana
Publisher : Indonesian Society for Biochemistry and Molecular Biology

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.32889/actabioina.217

Abstract

Background: Malaria is a life-threatening infectious disease caused by Plasmodium parasites, transmitted through infected female Anopheles mosquitoes. PfCyRPA (Plasmodium falciparum Cysteine-Rich Protective Antigen) has emerged as a promising vaccine candidate due to its ability to elicit inhibitory antibodies against parasite growth. Objective: This study aimed to construct recombinant plasmids encoding PfCyRPA fragment 26–181 and express this fragment in Escherichia coli BL21 CodonPlus (DE3) RIPL for cost-effective antigen production. Methods: The PfCyRPA gene fragment (~480 bp) was amplified from P. falciparum genomic DNA (Jayapura isolate) by PCR. Recombinant plasmids pGEM-T-PfCyRPA 26-181 and pET-16b-PfCyRPA 26-181 were constructed and confirmed via colony PCR, restriction analysis, and sequencing. The pET-16b-PfCyRPA 26-181 was transformed into E. coli BL21 CodonPlus (DE3) RIPL. Protein expression was induced with 0.5 mM IPTG at 37°C, and analyzed by SDS-PAGE and Western blotting. Results: SDS-PAGE and Western blot analysis demonstrated successful expression of recombinant PfCyRPA fragment 26–181 with a molecular mass of approximately 21.53 kDa, corresponding to the predicted size. The protein was predominantly expressed as inclusion bodies, typical for eukaryotic proteins in prokaryotic systems. Colony PCR and sequencing confirmed correct gene insertion and integrity. Conclusion: Recombinant PfCyRPA fragment 26–181 was successfully expressed in E. coli BL21 CodonPlus (DE3) RIPL, providing a cost-effective platform for large-scale antigen production. This work establishes a foundational protocol for further immunogenicity research and supports development of this antigen as a potential blood-stage malaria vaccine candidate.
New Pyrrole-Chalcone Hybrids Against Acetylcholinesterase: Synthesis, In Vitro, and Computational Studies Ridwanuloh, Dadan; Danova, Ade; Hermawati, Elvira; Chavasiri, Warinthorn; Ihsanawati, Ihsanawati; Alni, Anita
Journal of Multidisciplinary Applied Natural Science Articles in Press
Publisher : Pandawa Institute

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.47352/jmans.2774-3047.375

Abstract

Acetylcholinesterase (AChE) inhibition remains a central therapeutic approach for Alzheimer’s disease (AD), as it helps preserve synaptic acetylcholine levels, enhances cholinergic neurotransmission, and mitigates early cognitive decline. In this study, eight novel pyrrole–chalcone hybrids (3–10), consisting of four pyrrole–chalcones (3–6) and four pyrrole–chalcone amides (7–10), were designed, synthesized, and biologically evaluated for AChE inhibition. Among them, compound 8 (N-(4-methoxybenzyl)-pyrrole–chalcone amide) and compound 10 (N-(3,4-dimethoxybenzyl)-pyrrole–chalcone amide) demonstrated the strongest inhibitory activity, with IC₅₀ values of 3.1 and 2.8 µM, respectively, comparable to galantamine. Kinetic assays confirmed that both compounds act as noncompetitive inhibitors, as indicated by reduced Vmax without significant alteration in Km, while compound 10 exhibited Ki of 0.8 µM, reflecting high enzyme affinity. Molecular docking revealed strong binding interactions of compounds 8 and 10 with key AChE residues (Trp84, Phe330, Tyr334), supported by π–π stacking, π–alkyl interactions, and hydrogen bonding, with binding energies of –9.2 (compound 8) and –8.9 kcal/mol (compound 10). Molecular dynamics simulations further demonstrated that compound 10 forms a more stable and compact complex with AChE, as indicated by consistent RMSD values and a stable radius of gyration. SwissADME analysis confirmed favorable pharmacokinetic profiles for both ligands, including Lipinski compliance, high GI absorption, and absence of PAINS alerts, despite the lack of predicted BBB permeability. Overall, compound 10 emerges as the most promising noncompetitive AChE inhibitor in this series, exhibiting strong binding affinity, structural stability, and drug-likeness, thus warranting further optimization and in vivo evaluation.
Co-Authors Anita Alni, Anita Chavasiri, Warinthorn Cica Kasipah, Cica Danova, Ade DESSY NATALIA Hermawati, Elvira Masduki, Fifi Fitriyah Prameswari, Aurelia Galih Puspasari, Fernita Ridwanuloh, Dadan Setyowati, Widiastuti Agustina Eko Sinta Rismayani, Sinta ZEILY NURACHMAN