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ETIKA DAN TANGGUNG JAWAB KECERDASAN BUATAN (AI) DI PERPUSTAKAAN: TINJAUAN LITERATUR Komari, Noer; Fahruraji, Fahruraji; Noorliana, Noorliana; Asnah, Asnah
Jurnal Informasi, Perpustakaan, dan Kearsipan (JIPKA) Vol 5, No 1 (2025): Desember 2025
Publisher : Jurnal Informasi, Perpustakaan, dan Kearsipan (JIPKA)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.26418/jipka.v5i1.97978

Abstract

Integrasi kecerdasan buatan (AI) dalam layanan perpustakaan berkembang pesat seiring kemajuan model bahasa besar (LLM) dan teknologi pembelajaran mesin. AI menawarkan peluang untuk meningkatkan pengalaman pengguna, mengotomatisasi tugas rutin, serta menyediakan dukungan berkelanjutan. Namun, penerapannya juga menghadirkan tantangan etika dan profesional yang kompleks. Penelitian ini menyajikan tinjauan literatur menggunakan kerangka kerja PICO yang dimodifikasi, dengan menganalisis publikasi akademik periode 2020"“2025 yang diindeks dalam Google Scholar. Fokus kajian diarahkan pada empat isu utama: privasi data dan kerahasiaan pengguna, kebebasan intelektual dan integritas informasi, inklusi digital dan aksesibilitas, serta tanggung jawab profesional dalam kolaborasi manusia-AI. Hasil analisis menunjukkan bahwa meskipun perpustakaan masih berada pada tahap awal adopsi AI, persoalan etika sudah muncul secara mendesak. Tantangan utama meliputi risiko kebocoran data dan praktik pengintaian, potensi penyebaran misinformasi melalui sensor otomatis, meningkatnya kesenjangan digital, serta ketiadaan kerangka akuntabilitas yang tegas terhadap kesalahan AI. Temuan ini menegaskan bahwa pergeseran peran pustakawan dari sekadar penjaga informasi berubah menjadi kolaborator AI sekaligus auditor etika. Penelitian ini menyimpulkan bahwa profesi kepustakawanan perlu mengembangkan konsep augmented librarianship, membentuk kode etik baru yang relevan dengan penggunaan AI, serta mendorong transparansi dan akuntabilitas dari pengembang maupun penyedia teknologi. Dengan berpegang pada nilai inti, pustakawan memiliki posisi strategis untuk memastikan AI dimanfaatkan sebagai kekuatan yang memperkuat misi perpustakaan: menyediakan akses yang adil, etis, dan berintegritas terhadap pengetahuan bagi semua kalangan.
STRUCTURAL DYNAMICS OF BACTERIAL NITROREDUCTASE ENZYMES FROM A MINING-IMPACTED ENVIRONMENT IN SOUTH KALIMANTAN, INDONESIA: ARCHITECTURE FOR SUSTAINABLE CHROMIUM BIOREMEDIATION Anugerah Putra, Andifa; Ramadhani, Munandar; Komari, Noer; Badruzsaufari
BIOTROPIA Vol. 33 No. 1 (2026): BIOTROPIA Vol. 33 No. 1 January 2026
Publisher : SEAMEO BIOTROP

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11598/btb.2026.33.1.2532

Abstract

ARTICLE HIGLIGHTS- New bacterial enzymes found in Indonesian soil can neutralize toxic chromium waste.- These unique bacteria show great promise for bioremediation in polluted mining soils.- One of the newly found enzymes from these bacteria has a superior, highly stable structure.- This superior stability is key, coming from a rigid core with flexible moving loops.- This research provides a molecular blueprint for engineering enzymes to clean up chromium.ABSTRACTHexavalent chromium [Cr(VI)], a soluble and carcinogenic industrial pollutant, poses a significant threat to both the environment and human health, necessitating effective remediation strategies. Microbial enzymatic reduction of Cr(VI) to its less toxic trivalent state, Cr(III), is a promising approach. However, growing evidence suggests that many enzymes involved in this process are flavin mononucleotide (FMN)-dependent reductases, which likely reduce Cr(VI) adventitiously via a reduced flavin intermediate, rather than through direct enzymatic catalysis. This study presents a comparative computational analysis of two novel FMN-dependent reductases, designated M2Cr10 and M54Cr10, derived from chromium-tolerant bacteria Acinetobacter radioresistens and Bacillus tropicus, respectively, which were isolated from Indonesian serpentine soil. Phylogenetic and sequence analyses classified both enzymes as members of the FMN-dependent nitroreductase superfamily. High-quality homology models were generated and validated, with over 95% of residues occupying the most favored regions of the Ramachandran plot, confirming their stereochemical integrity. Molecular docking simulations predicted strong binding affinities for the FMN cofactor, with binding energies of -7.1 kcal/mol for M2Cr10 and -8.1 kcal/mol for M54Cr10. These interactions are stabilized by a network of hydrogen bonds and hydrophobic contacts, with residue Tyr¹³¹ identified as a key anchor for the FMN isoalloxazine ring in both enzymes. Extensive 10-nanosecond molecular dynamics simulations revealed that the A. radioresistens M2Cr10 enzyme exhibits superior structural architecture characterized by greater global stability, as indicated by lower average root mean square deviation (RMSD) and solvent-accessible surface area (SASA). However, it also displays greater localized flexibility (higher RMSF) in functional loop regions critical for catalysis. This combination of a rigid scaffold and dynamic functional loops suggests that M2Cr10 may be a more robust and potentially efficient biocatalyst. These findings provide a detailed molecular blueprint for understanding the structural determinants of stability in FMN-dependent reductases and offer a rational basis for engineering these enzymes for more effective adventitious bioremediation of Cr(VI).
Co-Authors A.A. Ketut Agung Cahyawan W Abdullah Abdullah Adi Rahmadi Afdella, Nor Afni Ahmad Budi Junaidi Akmal Rizky Harun Amalia Khairunnisa Aminuddin Prahatama Putra Anang Kadarsah Anang Kadarsah, Anang Anjang Yudistri Annisa Rizqi Dwi Oktaviani Anugerah Putra, Andifa An’nisa, Windy Sidratul Asnah Asnah Awin Fauzi Azidi Irwan Badruzsaufari Bambang Setiawan Dahlena Ariyani Desiya Ramayanti Azhara Dewi Umaningrum Diah Aulia Rosanti Dona Marisa, Dona Dwi Rasy Mujiyanti Dwi Rasy Mujiyanti Dwi Rasy Mujiyanti Eko Suhartono Eko Suhartono Erfanur Adlhani Etty Novita Fahruraji, Fahruraji Febriyanti, Nur Fatma Fitri Hady Amrullah Habibah, Hanna HANNA HABIBAH Hanna Habibah Ina Risnawati INDAH SAPUTRI Indah Saputri INDAH SETIAWATI Indah Setiawati Kamilia Mustikasari Karlina Karlina Khoerul Anwar Kholifatu Rosyidah Laksono Trisnantoro Lisda Hayatie, Lisda Lusi Thenios Mardi Santoso Maria Dewi Astuti Marisa Shellyanti Megayulia Nooryaneti Melina Arini Sylvia Dewi Mirza Maulana Ahmad Mukarramah Mukarramah, Mukarramah Nadia Sasanti NAFISAH Nafisah Nafisah Nafisah Nafisah Ningtyas Indah Sari Noor Malinda Noorliana Noorliana Nurhidayati Pratiwi Prahatama Putra, Aminuddin Puji Astuty Putra, Andifa Anugerah Putri, Amaris Nathania Hanindia Rabiatul Adawiyah Rahmat Eko Sanjaya Rahmi Hardini Ramadhani, Munandar Retno Agnestisia ROBIATUL ADAWIYAH Rusdiana Rusdiana Rusdiana Rusdiana Salmon Charles Pardomuan Tua Siahaan Samsul Hadi Samsul Hadi Samsul Hadi Saputri, Indah SARMILA Sarmila Sarmila Sarmila, Sarmila Siti Juliati Siti Ratna Jinan F Sri Hendriani Sujatmiko Sujatmiko Sujatmiko Sujatmiko Sunardi Sunardi Sunardi sunardi sunardi Sunardi, Ph.D., Sunardi Taslim Ersam Tri Ayu Novelena Umi Baroroh Lili Utami Utami Irawati Veronica Shania Aprillia Widiyanto, Gregorius Yenny Era Nova