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All Journal Indonesian Journal of Biotechnology Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology Jurnal SOLMA JSFK (Jurnal Sains Farmasi & Klinis) Jurnal Sains dan Kesehatan
Pertiwi, Wulan
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Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemistry Environmental Science Health Professions Immunology & microbiology Materials Science & Nanotechnology Medicine & Pharmacology Public Health Other

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Pengelolaan Sampah Organik Rumah Tangga Dengan Teknik “Octaco” Pada Kelompok PKK RW.05 Cipadung Kidul Kota Bandung Muharram, Luthfia Hastiani; Pertiwi, Wulan; Marlida, Siti; Wafa, Wafa; Nursafitri, Siti; Rachman, Indriyani; Matsumoto, Toru
Jurnal SOLMA Vol. 13 No. 3 (2024)
Publisher : Universitas Muhammadiyah Prof. DR. Hamka (UHAMKA Press)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22236/solma.v13i3.16400

Abstract

Background: Mengompos dapat diandalkan sebagai teknik mengolah sampah organik skala rumah, namun dalam praktiknya masih banyak kendala yang dihadapi. Perlu adanya inovasi teknik mengompos sehingga mudah dipraktikkan secara berkesinambungan oleh masyarakat. Pengurus PKK dapat menjadi penggerak dan percontohan dalam pengelolaan sampah rumah tangga. Salah satu inovasi mengompos yang sedang dikembangkan adalah Octaco (Octagonal Composter). Octaco merupakan inovasi teknik pengomposan sampah organik yang mudah dilakukan pada skala rumah tangga di perkotaan. Program pengabdian masyarakat ini bertujuan untuk meningkatkan keterampilan warga dalam mengelola sampah organik rumah tangga dengan pengomposan dengan teknik Octaco sehingga dapat mengurangi timbulan sampah. Metode: Metode program ini meliputi sosialisasi program dan Focus Group Discussion (FGD), pelatihan TOT (Training for Trainer) mengompos dengan teknik Octaco, dan pendampingan mengompos pada pengurus PKK RW 05 Cipadung yang berjumlah 16 orang. Pengabdian ini dilakukan selama bulan Juni - September 2024. Hasil: Hasil dari program pengabdian ini adalah sebanyak 100% peserta (16 orang pengurus PKK) telah berhasil melakukan pengomposan sampah organik rumah tangga dan memanfaatkan pupuk kompos untuk berkebun di rumah maupun di kebun komunitas, serta menggunakan kembali kompos untuk mengompos. Pengurus PKK yang sudah terlatih menjadi pelatih dan mendampingi warga lainnya dalam mengompos di rumah sehingga diharapkan semua warga dapat mengelola sampah organik secara mandiri dari rumah. Kesimpulan: Inovasi Octaco dapat direkomendasikan sebagai teknik mengompos yang mudah dilakukan pada skala rumah tangga. Keberhasilan mengompos yang berkesinambungan perlu berkolaborasi dengan komunitas setempat.
Prediksi Struktur 3D L-Asparaginase Bakteri Laut Vibrio sp. AND4 dengan Metode Homology Modelling Pertiwi, Wulan; Muharram, Luthfia Hastiani; Maulana, Farhan Azhwin
JSFK (Jurnal Sains Farmasi & Klinis) Vol 9 No 2 (2022): J Sains Farm Klin 9(2), Agustus 2022
Publisher : Fakultas Farmasi Universitas Andalas

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.25077/jsfk.9.2.121-128.2022

Abstract

L-asparaginase merupakan enzim yang menghidrolisis L-asparagin menjadi L-aspartat dan ammonia yang dapat digunakan dalam terapi pengobatan Leukemia Limfoblastik Akut. Penentuan struktur 3D L-asparaginase dari berbagai sumber dapat memberikan informasi penting dalam memahami sifat dan fungsi biokimia L-asparaginase di level molekuler untuk penelusuran L-asparaginase alternatif sebagai protein teurapetik. Tujuan penelitian ini adalah memprediksi struktur 3D enzim L-asparaginase II dari bakteri laut Vibrio sp. AND4 dengan E.coli L-asparaginase II mutant (T12V) in complex with L-Asn at pH 7.0 [Escherichia coli K-12] (PDB ID: 6PA9) sebagai templat struktur, menggunakan metode pemodelan homologi dengan program SWISS-MODEL. Penelitian ini menghasilkan model struktur 3D dengan Sequence identity 70,55%, memiliki nilai QMEANDisCo 0,86±0,05 dan nilai GMQE sebesar 0,86. Terdapat 93,1% residu berada di daerah the most favored regions dan 0,3% residu berada di daerah disallowed regions pada Ramachandran plot, dengan G-Factors sebesar -0.08 yang memenuhi syarat-syarat kualitas struktur ideal.
Marine Bacteria Producing L-Asparaginase with Low Glutaminase and Urease Co-Activity from Pangandaran East Coast Indonesia Pertiwi, Wulan; Namira, Azmy Jasmine; Moeis, Maelita Ramdani; Muharram, Luthfia Hastiani; Hernahadini, Nelis
Squalen, Buletin Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 20, No 1 (2025): May 2025
Publisher : :Agency for Marine and Fisheries Research and Human Resources, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/squalen.908

Abstract

acterial L-asparaginase is a therapeutic enzyme widely used in the treatment of Acute Lymphoblastic Leukemia (ALL). Although L-asparaginase is prominent in treating ALL, its use is limited due to its side effects caused by its dual substrate specificity towards both asparagine and glutamine. This study aimed to isolate and identify marine bacteria from the East Coast of Pangandaran capable of producing L-asparaginase with low glutaminase and urease co-activities. A semi-quantitative approach was employed, involving the isolation and screening of seawater bacteria using Zobell Marine media supplemented with L-asparagine, glutamine or urea and phenol red as a pH indicator to determine the enzymatic activity. Molecular identification was performed by amplifying and sequencing the 16S rRNA gene, followed by phylogenetic analysis using the neighbor-joining method with 1,000 bootstrap replicates. The results indicated that the bacterial isolate designated PT3 exhibited a high enzymatic index of 4.2 for L-asparaginase, surpassing that of the positive control (E. coli), which had an index of 1.4. Sequence analysis revealed that PT3 shared 99.58% identity with Marinobacterium georgiense strain NBRC 102606, an earlier synonym of Marinobacterium iners. Therefore, PT3 was identified as a strain of Marinobacterium iners, with potential as a novel source of L-asparaginase and displayed significant L-asparaginase activity with minimal co-activity of glutaminase and urease, highlighting its potential as a safer alternative for therapeutic enzyme development.
Aktivitas Gelatinase Bakteri Endogen Maggot Black Soldier Fly (Hermetia illucens) pada Hydrolyzed Collagen (HC) yang Berasal dari Limbah Pengolahan Ikan Tuna: Gelatinase Activity of Endogenous Bacteria of Maggot Black Soldier Fly (Hermetia illucens) on Hydrolyzed Collagen (HC) Derived from Tuna Fish Processing Waste Ismi, Alfita Ramdiyati; Aisah, Aisah; Sheptiriani, Amelia Firdia; Amelia, Rena Pitri; Nada, Qatrun; Syaputri, Fauzia Ningrum; Pertiwi, Wulan
Jurnal Sains dan Kesehatan Vol. 7 No. 5 (2025): J. Sains Kes.
Publisher : Fakultas Farmasi, Universitas Mulawarman, Samarinda, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.25026/jsk.v7i5.2451

Abstract

Hydrolyzed collagen (HC) is an enzymolyzed collagen or gelatin product and has a small molecular weight (0.3-8 kDa). HC can be produced enzymatically with protease enzymes. The methods used in HC production include isolation of gelatinase-producing bacteria from BSF maggots, gelatin extraction from tuna fish waste, gelatinase activity screening, gelatinase enzyme production, HC production, and confirmation analysis. Bacterial isolation resulted in 22 bacterial colonies, 3 of which had gelatinase activity as observed from the activity screening results. The yield of gelatin extract obtained was 9.36%. HC production was obtained as much as 10 mL with the addition of 5% crude gelatinase enzyme. The SDS-PAGE results can be determined that there is a band with a size of 31-42 kDa, it shows that the gelatinase can be isolated. Keywords:          hydrolyzed collagen, maggot BSF, tuna fish, gelatinase, gelatin   Abstrak Hydrolyzed collagen (HC) merupakan produk kolagen atau gelatin yang terenzimolisis dan memiliki ukuran berat molekul yang kecil (0,3-8 kDa). HC dapat diproduksi secara enzimatik dengan enzim protease. Metode yang digunakan dalam produksi HC antara lain adalah isolasi bakteri penghasil gelatinase dari maggot BSF, ekstraksi gelatin dari limbah ikan tuna, skrining aktivitas gelatinase, produksi enzim gelatinase, produksi hydrolyzed collagen, dan analisis konfirmasi. Isolasi bakteri didapatkan koloni bakteri sebanyak 22 koloni, 3 diantaranya memiliki aktivitas gelatinase yang diamati dari hasil skrining aktivitas, Rendemen ekstrak gelatin yang didapatkan adalah 9,36%. Produksi HC didapatkan sebanyak 10 mL dengan penambahan 5% crude gelatinase enzyme. Hasil SDS-PAGE dapat ditentukan bahwa terdapat pita pada ukuran 31-42 kDa, hal ini menunjukkan bahwa gelatinase dapat terisolasi. Kata Kunci:         hydrolyzed collagen, maggot BSF, ikan tuna, gelatinase, gelatin
Recombinant expression and preliminary characterization of a synthetic L‐asparaginase from the marine bacterium Pseudoalteromonas tetraodonis GFC in Escherichia coli BL21 (DE3) Pertiwi, Wulan; Tohari, Taufik Ramdani; Suhada, Qori Atur Rodiah; Zahira, Tiara; Nugraha, Nadila Suci
Indonesian Journal of Biotechnology Vol 31, No 1 (2026)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.114307

Abstract

The marine environment represents a promising source of diverse enzymes produced by marine microorganisms, including L‐asparaginase. This has been widely studied due to its ability to hydrolyze extracellular L‐asparagine, an amino acid required for the growth of certain cancer cells. In this study, a synthetic L‐asparaginase gene derived from the marine bacterium Pseudoalteromonas tetraodonis GFC was recombinantly expressed in Escherichia coli BL21 (DE3). The gene was cloned into the pD861‐SR expression vector and transformed into E. coli BL21 (DE3). Positive transformants were confirmed by restriction digestion using SapI and Sanger sequencing. Recombinant protein expression was induced with L‐rhamnose under the control of the rhaBAD promoter. The expressed L‐asparaginase was then purified using Ni‐Sepharose affinity chromatography followed by membrane dialysis, yielding a protein purity of 73.6%. SDS‐PAGE analysis revealed a prominent protein band at approximately 37 kDa, corresponding to the expected molecular weight of recombinant L‐asparaginase. Enzymatic activity was evaluated using the Nessler method, and the purified enzyme exhibited a specific activity of 5.863 U/mg. These results demonstrate the successful recombinant expression and preliminary functional validation of L‐ asparaginase from P. tetraodonis GFC in E. coli, providing a basis for further optimization and characterization in future studies.
Co-Authors Aisah Aisah Amelia, Rena Pitri Fauzia Ningrum Syaputri, Fauzia Ningrum Hernahadini, Nelis Indriyani Rachman Ismi, Alfita Ramdiyati MAELITA RAMDANI MOEIS Marlida, Siti Matsumoto, Toru Maulana, Farhan Azhwin Muharram, Luthfia Hastiani Nada, Qatrun Namira, Azmy Jasmine Nugraha, Nadila Suci Nursafitri, Siti Sheptiriani, Amelia Firdia Suhada, Qori Atur Rodiah Tohari, Taufik Ramdani Wafa, Wafa Zahira, Tiara