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All Journal Makara Journal of Science Environmental and Materials
Hanzhola Gusman Riyanto
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Chemical Engineering, Chemistry & Bioengineering Control & Systems Engineering Energy Engineering Physics

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Journal : Makara Journal of Science

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Preliminary Molecular Study of Chloramphenicol Anchoring on Laccase Enzyme from Trametes hirsuta Riyanto, Hanzhola Gusman; Sanjaya, Afiten Rahmin
Makara Journal of Science Vol. 28, No. 3
Publisher : UI Scholars Hub

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Abstract

Antibiotics are one of emerging pollutants generally emitted from livestock production and the food industry to the environment. The presence of this pollutant could initiate the development of resistant bacteria that can be fatal to human health. The degradation of antibiotics using enzymes or microbe could be an alternative because the residue or intermediate product is less harmful than of the conventional method. This research aims to support a preliminary study of the degradation of antibiotics using enzyme through molecular docking via Molecular Operating Environment software and molecular dynamics (MD) study via CABSFLEX 2.0 and WebGro macromolecular simulations. The molecular docking of the laccase-chloramphenicol complex has low binding energies of approximately −8.1350 and −8.2290 kcal/mol for both rigid and flexible methods, respectively, indicating that the formation of the complex is advantegous. MD simulation further revealed a decrease in rigidity after the interaction with the ligand. Hydrogen bonding analysis indicated up to five hydrogen bonds in the complex, underscoring the robustness of the enzyme--ligand interaction. These results collectively contribute to our understanding of the efficacy of enzyme-mediated antibiotic degradation and emphasize the potential for this approach to mitigate environmental and health concerns associated with antibiotic pollution
Microplastic Degradation using Laccase Enzyme from Trametes hirsuta: In the Silico Study Riyanto, Hanzhola Gusman; Sylvia, Diana
Makara Journal of Science Vol. 29, No. 4
Publisher : UI Scholars Hub

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Microplastics are a serious global problem that arises worldwide because of their widespread use. Exposure to microplastics can negatively affect human and environmental health. In this study, we used molecular docking methods with MOE software (version 2014.0901) to investigate the interaction between the laccase enzyme and several microplastic compounds as a preliminary study of microplastic degradation using enzymes. The Quantitative Structure Analysis Relationship (QSAR) analysis revealed that all microplastic ligands had higher Pa values than Pi, indicating that the laccase enzyme may be biologically active. The findings of the present study show that polyamide (PA) has the lowest binding energy among microplastics, implying that the enzyme can interact well with both active sites. In contrast, polypropylene exhibited the highest binding energy, indicating a lack of strong residue interactions between the ligand and the active sites. The Phe463 active site work well when dealing with nonpolar aromatic polymers, including polycarbonate, poly (methyl methacrylate), polystyrene, and polyurethane, allowing for significant π–π stacking interactions. The Ile455 active sites are more effective when dealing with polar aromatic polymers, such as PET and polyamide, due to their better hydrogen bonding or dipole interactions. This finding can be used as an initial basis for microplastic enzymatic degradation
Co-Authors Afiten Rahmin Sanjaya Dede Nurhalimah ENDANG SAEPUDIN Endang Saepudin, Endang Isnaini Rahmawati Nurhalimah, Dede Octaviany Magdalena Pasaribu, Lewita Putri, Yulia Mariana Tesa Ayudia Rachman, Fathur Rahmawati, Isnaini Sanjaya, Afiten Rahmin Sylvia, Diana Tesla, Yudistira Yudistira Tesla Yulia Mariana Tesa Ayudia Putri Yuni Krisyuningsih Krisnandi Yuni Krisyuningsih Krisnandi, Yuni Krisyuningsih