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All Journal HAYATI Journal of Biosciences Microbiology Indonesia Indonesian Journal of Biotechnology Jurnal Bioteknologi & Biosains Indonesia (JBBI) Jurnal Biodjati Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology TROPICAL GENETICS Tropical Genetics
MAELITA RAMDANI MOEIS
School Of Life Sciences And Technology, Institut Teknologi Bandung, Jalan Ganesha 10, Bandung 40132, Indonesia
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Computer Science & IT Decision Sciences, Operations Research & Management Earth & Planetary Sciences Environmental Science Immunology & microbiology Materials Science & Nanotechnology Medicine & Pharmacology

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Expression and Purification of PhoR Sensor-Domain Histidine Kinase of Mycobacterium tuberculosis in Escherichia coli ERNAWATI ARIFIN GIRI-RACHMAN; FENRYCO PRATAMA; OKTIRA ROKA AJI; ARUM PATRIATI; IHSANAWATI IHSANAWATI; MAELITA RAMDANI MOEIS; EDY GIRI-RACHMAN PUTRA
Microbiology Indonesia Vol. 9 No. 2 (2015): June 2015
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1382.183 KB) | DOI: 10.5454/mi.9.2.1

Abstract

Globally, tuberculosis (TB) remains a leading cause of death. The emergence of multidrug-resistant strains (MDR-TB) and extensively drug-resistant strains (XDR-TB) has fuelled the discovery for novel drugs and drug targets for its successful and better treatment. One of the potential candidates for drug target is PhoR sensory protein histidine kinase, a part of the Two Component System (TCS) PhoP/PhoR in Mycobacterium tuberculosis (Mtb). This protein system was known for its role on regulating hundred of Mtb virulence factors, from genes for cell wall and lypid synthesis to genes for adaptation in human leukocyte and hypoxia response. Previous studies have successfully characterized, isolated, and cloned the putative sensory domain of PhoR protein gene into pRSET vector expression system. In this study, Escherichia coli was transformed with pRSET-SensPhoR and cultivated at 37oC under IPTG induction to express PhoR sensor-domain protein. Most of the proteins were overexpressed in the form of inclusion bodies.  Subsequent protein purification in Ni-NTA system under refolding condition on urea gradient was performed to isolate PhoR sensor-domain protein in soluble form. Arginine was supplemented in purified protein solution to prevent aggregation during long term storage.  While highly purified protein was acquired, small angle X-ray scattering (SAXS) analysis was conducted to obtain 3-dimensional (3D) protein structures in solution.    doi:10.5454/mi.9.2.1 
Identification of single nucleotide polymorphisms on the D-loop region of mtDNA in Sundanese population Wolly Candramila; Sony Heru Sumarsono; Bambang Suryobroto; Maelita Ramdani Moeis
Tropical Genetics Vol. 1 No. 1 (2021)
Publisher : Genetikawan Muda Indonesia

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Abstract

Identification of sequence polymorphism on the D-loop region of mtDNA has been done for various purposes, including health and medical treatment. In this research, single nucleotide polymorphisms were identified in the D-loop region of mtDNA of the Sundanese population in western Java. A total of 118 unrelated and healthy Sundanese probands were collected from closed-traditional kampung adat and open communities distributed in 14 cities and regencies in western Java. DNA amplification and direct sequencing of the D-loop region were proceeded using primers L15990 and H409. Multi-alignment was conducted not only intrapopulation but also with D-loop sequence data stored in GenBank for comparison. In this research, we categorized high-frequency SNPs as less effective for identification in population studies because of their presence in other populations outside Indonesia. Meanwhile, lower-frequency SNPs showed typical variants of Sundanese haplotypes. On the other hand, rare or low-frequency SNPs should be re-examined in larger size of samples to have a better understanding of risk factors for many diseases.
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.
Extracellular β-Glucosidase Production from bglp15.2 Gene Carrying Inulinase Signal Peptide in Saccharomyces cerevisiae BY4741 Armaya Badiatul Fitri; Elvi Restiawaty; Maelita Ramdani Moeis
Jurnal Biodjati Vol 2 No 2 (2017): November
Publisher : UIN Sunan Gunung Djati Bandung

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15575/biodjati.v2i2.1619

Abstract

One of the important enzymes in cellulase complex is β-glucosidase. In this research, adding signal peptide of inulinase gene from Kluyveromyces marxianus, cloning, and expressing of bglp15.2 gene in S. cerevisiae BY4741 had been done. Gene of bglp15.2 encoding β-glucosidase has 90% identity to nucleotide sequence of Shewanella frigidimarina NCIMB 400 bacteria. Adding nucleotide sequence of signal peptide was aimed to secrete β-glucosidase and had been done with PCR (Polymerase Chain Reaction) method. The addition of nucleotide sequence of signal peptide in bglp15.2 gene had been done succesfully that indicated from nucleotide sequencing result and the increment of amplicon band size in electroferogram of the last addition PCR step. The bglp15.2 and bglp15.2INU gene (the bglp15.2 gene that has signal peptide nucleotide sequence) were cloned in Escherichia coli DH5α using pGEM-T-Easy vector and pBEVY-GL shuttle vector. The pBEVY-GL shuttle vector was used for transforming S. cerevisiae BY4741 with bglp15.2 and bglp15.2INU. The recombinant S. cerevisiae BY4741 carrying bglp15.2INU gene and growing in 48 hours had extracellularly β-glucosidase enzyme activity of 0,0178 U/ml and the intracellularly activity was 0,0181 U/ml. The  β-glucosidase enzyme without signal peptide was not secreted. With K. marxianus inulinase signal peptide, about 50% Bglp15.2INU protein could be secreted. The protein molecular weight of secreted Bglp15.2INU was 44 kDa in SDS-PAGE result.
Co-Authors ARI DWIJAYANTI Armaya Badiatul Fitri ARUM PATRIATI Bambang Suryobroto DESSY NATALIA Edvan Arifsaputra Suherman EDY GIRI-RACHMAN PUTRA EDY SANWANI Elvi Restiawaty Elvi Restiawaty ERNAWATI ARIFIN GIRI-RACHMAN FENRYCO PRATAMA Hans Victor Hernahadini, Nelis Ihsanawati Ihsanawati Mochamad Untung Kurnia Agung Muharram, Luthfia Hastiani Namira, Azmy Jasmine Oktira Roka Aji Pertiwi, Wulan RAHMA WIDYA NINGRUM SAKINAH HASNI SITI KHODIJAH CHAERUN SONY HERU SUMARSONO SONY HERU SUMARSONO Victor, Hans Victor, Hans WOLLY CANDRAMILA