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All Journal HAYATI Journal of Biosciences Microbiology Indonesia JURNAL KESEHATAN LINGKUNGAN: Jurnal dan Aplikasi Teknik Kesehatan Lingkungan
FENRYCO PRATAMA
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Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Earth & Planetary Sciences Immunology & microbiology Medicine & Pharmacology Public Health

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Cloning, Overexpression, and Purification of PhoR CytoplasmicDomain Protein from Mycobacterium tuberculosis strain H37Rv OKTIRA ROKA AJI; DYSHELLY NURKARTIKA PASCAPURNAMA; FENRYCO PRATAMA; IHSANAWATI IHSANAWATI; MAELITA RAMDHANI MOEIS; ERNAWATI ARIFIN GIRI-RACHMAN
Microbiology Indonesia Vol. 8 No. 4 (2014): December 2014
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (758.166 KB) | DOI: 10.5454/mi.8.4.1

Abstract

Tuberculosis still becomesa major health problem in the world. This infectious disease is caused by Mycobacterium tuberculosis (Mtb). Novel anti-tubercular drug is urgently needed to counter multidrug resistant cases and Mtb's spread. The cytoplasmic domain of PhoR histidine kinase, a part of the two-component system PhoR-PhoP in Mtb, is one of the potential candidates for anti-tubercular drug target.Three dimensional protein of drug target is needed to screen potential drug candidate using rational drug design approaches. Previous studies have successfully characterized and isolated putative cytoplasmic domain of PhoR (CytoPhoR) from Mtb strain H37Rv. This study aimed to clone, overexpress and purify of CytoPhoR protein. CytoPhoR was fused with thioredoxin protein in expression vector pET32b and overexpressed in Escherichia coli (E.coli)BL21 (DE3) as soluble fraction by induction  1 mM IPTG. Purification of his-tagged CytoPhoR was carried out using IMAC Ni-NTA Agarose his-tag affinity column. SDS-PAGE analysis showed that another protein was co-purified (~35 kDa) along with the CytoPhoR protein. Subsequent protein purification using DEAE-ion exchange column generate a strong single band of 37 kDa on SDS–PAGE which is indicated as CytoPhoR protein. The purified CytoPhoR protein was successfully obtained and can be used for further analysis on determining three dimensional structure of CytoPhoR protein.
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 
Study of Contamination Control in The Pharmaceutical Industry: Ethylene Glycol and Diethylene Glycol Anugrah, Resmilia; Nurhalisa Kairupan, Daning; Liyana Putri, Fadhilah; Ulfa, Munira; Pratama, Fenryco
JURNAL KESEHATAN LINGKUNGAN: Jurnal dan Aplikasi Teknik Kesehatan Lingkungan Vol 20 No 2 (2023): Jurnal Kesehatan Lingkungan Volume 20 No. 2, Juli 2023
Publisher : Poltekkes Kemenkes Banjarmasin Jurusan Kesehatan Lingkungan Banjarbaru

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.31964/jkl.v20i2.653

Abstract

Contamination cases in health products are on the rise, mainly due to ethylene glycol and diethylene glycol contaminants, which contribute to the high number of child deaths. Contamination caused by toxic compounds should be controlled and minimized to ensure public safety and security. Therefore, contamination control needs further review. This paper aims to discuss HACCP and GMP procedures for controlling and minimizing contaminants in the pharmaceutical industry, as well as policies and coordination between actors to prevent the recurrence of cases of ethylene glycol and diethylene glycol contamination. The research used the literature study method, with hazing's publication or perish as a search tool. The results of this paper show that in the application of HACCP, there are several critical control points, namely the manufacture of drugs, the removal of materials, screening of raw materials, dry mixing, mixing, and packaging. GMP implements controls on sanitation and hygiene, equipment, self-inspection and supplier approval audits, personnel, training, personal hygiene, and locations and buildings. In order to prevent the recurrence of contamination cases, it is necessary to apply policies related to suppliers of raw materials, raw materials, and the application of GMP. Coordination between actors at the country and company scales is necessary to prevent the recurrence of ethylene glycol and diethylene glycol contamination cases.
Cloning and Optimized Expression of Bst DNA Polymerase from Geobacillus stearothermophillus in Escherichia coli BL21 Taufik, Intan; Fanany, Rizal; Manjaswari, Agika; Pratama, Fenryco
HAYATI Journal of Biosciences Vol. 32 No. 1 (2025): January 2025
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.32.1.155-163

Abstract

Bst DNA polymerase possesses strand displacement activity, enabling isothermal DNA amplification without requiring a thermal cycler. This enzyme is utilized in the Loop-Mediated Isothermal Amplification (LAMP) method, which offers advantages in speed and simplicity over Polymerase Chain Reaction (PCR) method. The growing demand for Bst DNA polymerase highlights the need for cost-effective in-house production, as a commercial option is economically challenging. For that purpose, this study aims to construct and optimize the expression of Bst DNA polymerase from Geobacillus stearothermophilus in Escherichia coli. The expression constructs pET16b.BstHF vector was constructed using Gibson Assembly and expressed in E. coli BL21 (DE3). Optimal expression was achieved with 1 mM IPTG, induction at OD600 0.8 and 6-hour induction time. The purified enzyme was achieved with a protein yield of 2,175 mg/L culture and demonstrated effective polymerase activity for LAMP.
Co-Authors Anugrah, Resmilia ARUM PATRIATI DYSHELLY NURKARTIKA PASCAPURNAMA EDY GIRI-RACHMAN PUTRA ERNAWATI ARIFIN GIRI-RACHMAN Fanany, Rizal IHSANAWATI IHSANAWATI Liyana Putri, Fadhilah MAELITA RAMDANI MOEIS MAELITA RAMDHANI MOEIS Manjaswari, Agika Nurhalisa Kairupan, Daning Oktira Roka Aji Taufik, Intan Ulfa, Munira