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All Journal HAYATI Journal of Biosciences Jurnal Agronomi Indonesia (Indonesian Journal of Agronomy) Jurnal Gizi dan Pangan Jurnal Fitopatologi Indonesia Jurnal Teknologi Dan Industri Pangan Jurnal Akuakultur Indonesia Jurnal Farmasi Udayana CHEMISTRY PROGRESS Jurnal Pendidikan Bahasa dan Sastra Indonesia Undiksha Microbiology Indonesia BIOTROPIA - The Southeast Asian Journal of Tropical Biology Current Biochemistry The Journal of Pure and Applied Chemistry Research Indonesian Journal of Biotechnology BERITA BIOLOGI ANNALES BOGORIENSES FITOFARMAKA: Jurnal Ilmiah Farmasi Menara Perkebunan Jurnal Jamu Indonesia Sainstek : Jurnal Sains dan Teknologi Jurnal Pusat Inovasi Masyarakat Jurnal Ilmu Kehutanan Molekul: Jurnal Ilmiah Kimia Journal of The Indonesian Society of Integrated Chemistry Indonesian Journal of Jamu Annales Bogorienses

I MADE ARTIKA

Department Of Biochemistry, Faculty Of Mathematics And Natural Sciences, Darmaga Campus, IPB University, Bogor, 16680, Indonesia

Author-ID : 234078

Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Computer Science & IT Decision Sciences, Operations Research & Management Earth & Planetary Sciences Economics, Econometrics & Finance Education Environmental Science Health Professions Immunology & microbiology Industrial & Manufacturing Engineering Languange, Linguistic, Communication & Media Materials Science & Nanotechnology Medicine & Pharmacology Social Sciences Veterinary Other

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Structural and Functional Analysis of FLAG Tagged-Subunit 8 of Yeast Saccharomyces cerevisiae Mitochondrial ATP Synthase I MADE ARTIKA
Microbiology Indonesia Vol. 1 No. 1 (2007): April 2007
Publisher : Indonesian Society for microbiology

Yeast mitochondrial ATP synthase is a multisubunit complex composed of at least 17 different subunits. Subunit 8 of yeast mitochondrial ATP synthase is a hydrophobic protein of 48 amino acids encoded by the mitochondrial ATP8 gene. Although ATP synthase from eukaryotes and prokaryotes shows a similar basic structure, no homologue of subunit 8 is found in prokaryotes such as Escherichia coli. Subunit 8 has three distinct domains; an N-terminal domain, a central hydrophobic domain and a C-terminal domain. In order to elucidate its structure and function, a set of nuclear genes encoding subunit 8 variants was designed to incorporate a FLAG tag at the C-terminus and a mitochondrial signal peptide at the N-terminus. Each gene was cloned into a yeast expression vector and then allotopically expressed in a yeast strain lacking endogenous subunit 8. Structural and functional analysis showed that the hydrophobic character of the central hydrophobic domain of subunit 8 is critical for the ATP synthase function. Subunit 8 is sensitive to charge manipulation at the C-terminus. The positively charged residues at the C-terminal domain are important for subunit 8 assembly and hence its function.

The Production of Tannin Acyl Hydrolase from Aspergillus niger YUNITA ARIAN SANI ANWAR; . HASIM; I MADE ARTIKA
Microbiology Indonesia Vol. 1 No. 2 (2007): August 2007
Publisher : Indonesian Society for microbiology

The aim of this research was to produce tannin acylhydrolase (tannase) from Aspergillus niger isolated from cacao pod. The first step of the study included determination of optimal pH, temperature, and incubation period to produce tannase. Optimal conditions obtained for tannase production were pH 5.5, a temperature of 28 oC and an incubation period of 3 days. Optimization of production medium was conducted. The media tested were solid and liquid wheat flour media with a concentration of tannic acid as inducer at 0, 3, 5, and 7% (wt/vol). The best production medium was solid medium with tannic acid concentration of 5% (wt/vol).

Membrane Topology of Subunit 8 Variant of Yeast Saccharomyces cerevisiae Mitochondrial ATP Synthase I MADE ARTIKA
Microbiology Indonesia Vol. 3 No. 1 (2009): April 2009
Publisher : Indonesian Society for microbiology

The yeast mitochondrial F1F0-ATP synthase is a multisubunit complex that contains at least 17 different subunits. Subunit 8 of yeast mitochondrial ATP synthase is a hydrophobic protein of 48 amino acids encoded by the mitochondrial ATP8 gene. There is no homologue of subunit 8 found in bacteria. Subunit 8 has three distinct domains; an N-terminal domain, a central hydrophobic domain and a C-terminal domain. Subunit 8 has been shown to adopt a transmembrane topology with the central hydrophobic domain spans the inner mitochondrial membrane once. In order to elucidate the need of subunit 8 to maintain transmembrane topology for its functioning, a severely functionally defective subunit 8 variant that has been introduced with double-charged residues within the central hydrophobic domain was analysed. A gene encoding this variant was expressed in a yeast strain lacking endogenous subunit 8. The subunit 8 variant was then targeted into mitochondria. Following its assembly into mitochondrial ATP synthase complex, its membrane topology was determined. The results obtained showed that subunit 8 was obligatory to maintain a transmembrane topology for providing proper functioning. The transmembrane topology may be critical for subunit 8’s proposed tructural roles as part of the stator stalk of the mitochondrial ATP synthase complex.

Bioenergetic Analysis of FLAG Tagged-Subunit 8 of Saccharomyces cerevisiae Mitochondrial ATP Synthase I MADE ARTIKA
Microbiology Indonesia Vol. 4 No. 3 (2010): December 2010
Publisher : Indonesian Society for microbiology

The majority of cellular energy in the form of adenosine triphosphate (ATP) is synthesized by the F1F0-ATP synthase. The yeast mitochondrial F1F0-ATP synthase is a multisubunit complex that contains at least 17 different subunits grouped into F1 and F0 sectors. Subunit 8 of yeast mitochondrial ATP synthase is a hydrophobic protein of 48 amino acids encoded by the mitochondrial ATP8 gene. Subunit 8 has three distinct domains; an N-terminal domain, a central hydrophobic domain and a C-terminal domain. FLAG tag addition to the C-terminus of subunit 8 and its variants has facilitated elucidation of subunit 8's membrane topology. In order to analyze its detailed structure and function, a set of strains expressing FLAG tagged-subunit 8 and its variants were subjected to bioenergetic analysis at cellular and mitochondrial levels. Results obtained showed that the hydrophobic character of the central hydrophobic domain of subunit 8 is essential for functional coupling between F1 and F0 sectors, hence for mitochondrial ATP synthase function.

Antibacterial Activity of Propolis Supplemented-Chewing Candy Against Streptococcus mutans I MADE ARTIKA; HARYANTO SUSILO; ADINDA VIRGINIA DWI SETYO; AHMAD ENDANG ZAINAL HASAN
Microbiology Indonesia Vol. 5 No. 3 (2011): September 2011
Publisher : Indonesian Society for microbiology

Streptococcus mutans is considered to play a major etiological role in development of human dental plaque believed to related to dental caries, the most prevalent disease of the human oral cavity. The objectives of the present study were to formulate and produce propolis supplemented-chewing candy and to investigate its antibacterial activity against S. mutans. Propolis is a natural resinous bee-hive product thought to have antimicrobial, anti-inflammatory and immunostimulating activities. Propolis was extracted from hives of bees of Trigona spp. using ethanol. The extract was coated with maltodextrine and homogenized to generate propolis microparticles. The particles were introduced into chewing candy preparations for the production of propolis supplemented-chewing candy. The candy was then subjected to in vitro antibacterial assays to test its activity against S. mutans isolated from human dental plaque. Results showed that the ethanol extracted propolis of Trigona spp. bee-hives can be homogenized to form propolis microparticles. The propolis microparticles could be used as a supplement in the formulation of chewing candy preparations. The propolis supplemented-chewing candy showed antibacterial activity against S. mutans. The candy, therefore, has the potential to be used as an antiplaque agent for prevention of dental caries.

Inhibitory activity of Lactobacillus plantarum U10 isolated from Tempoyak (fermented durian) Made in Indonesia against Salmonella typhi SOGANDI SOGANDI; APON ZAENAL MUSTOPA; I MADE ARTIKA; BUGI RATNO BUDIARTO
Microbiology Indonesia Vol. 9 No. 2 (2015): June 2015
Publisher : Indonesian Society for microbiology

Lactobacillus plantarum U10 produced bacteriocin U10 which was isolated from a traditionally fermented food â€œtempoyakâ€ from Sumatera Island in Indonesia. Production of the bacteriocins started at early exponential phase and reached maximum level at early stationary phase. Furthermore, plantaricins U10 was purified by ammonium sulphate precipitation followed by gel filtration chromatography. L. plantarum U10 produced two bacteriocins with a molecular mass of approximately 4.5 and 9.8 kDa by SDS-PAGE.Â The mode of action of plantaricins U10 was identified as bactericidal agents against Salmonella typhi ATCC25241 as proven by CFU counting and SEM micrographs that showed differences in cell structures between treated cells and the non-treated control. SEM examination also confirmed structural destruction of membrane cells integrity and considerable morphological alteration of S.typhi.

Co-Authors . SURYANI A. E. Zainal Hasan AA Sudharmawan, AA Abdillah, Ramadhani Malik Abdul Choliq ADINDA VIRGINIA DWI SETYO Agung Eru Wibowo Agung Eru Wibowo AHMAD ENDANG ZAINAL HASAN AHMAD ENDANG ZAINAL HASAN Ahmad Sulaeman Akhmad Endang Zainal Hasan Amanda, Nisa Widya AMIN FATONI Andani, Gita Putri Andita Fitri Mutiara Rizki, Andita Fitri Mutiara Antonius Padua Ratu Apipah Aprianti APON ZAENAL MUSTOPA Apon Zaenal Mustopa Arya Arendra Asri Sulfianti Azmi Azhari Azmi Azhari, Azmi Azmi, Wihda Aisarul BUGI RATNO BUDIARTO DEDI JUSADI Denny Irawati Desi Purwaningsih Dewi Sukma DIMAS ANDRIANTO Djarot Sasongko Hami Seno Dodi Safari Dodi Safari Dodi Safari Dodi Safari Dwi N. Susilowati Dzihan Dinar Rabani Eliza Halim Erismar Amri Erlank Bagjavicenna Erna Puspasari Evi Nur Qolbaini Fatriani, Rizka Fina Febrianti Firda DIMAWARNITA Firdausy, Iman Akhyar Firmansyah, Ridwan Putra Fri Rahmawati Gholam, Gusnia Meilin Gita Putri Andani Gusnia Meilin Gholam H. A. E. Zainal Hasan Hani 'Athiyya Rafi Hardinsyah Harsana, Ngurah HARTUTIK EKA SUSANTI HARYANTO SUSILO Hasim - HASIM DANURI Hayatul Rahmi Herti Sugiarti Herti Sugiarti, Herti Hyakansa HANIF Ifa Manzila Iman Rusmana Inawati Inawati Irsal, Riyan Alifbi Putera Jajang Suhyana K, Popi A kurnia agustini Kurnia Agustini Laita Nurjanah Laita Nurjanah, Laita LAKSMI AMBARSARI Lasmiyanti, Metty Lusiana Kresnawati Hartono Luthfi Ramadhani, Dhani Luzicoiij, Michael Edison M. Zairin Junior M.Pd Prof. Dr. I Nyoman Sudiana . Mala Nurilmala MARIA BINTANG Meilisza, Nina Melva Louisa Mirza Dikari Kusrini MS, Yulia Atika Muhaimin Muhaimin MUHAMMAD AGUS SUPRAYUDI Muhammad Dailami, Muhammad Muhammad Nafiz Nisa Widya Amanda Noorwati Sutandyo Norman Razief Azwar Norman Razief Azwar Novik Nurhidayat Novik Nurhidayat Nuke Annisa Nasution NUNUK WIDHYASTUTI Nur Bambang Priyo Utomo Nur Hasanah Nur Hasanah Nurmala Sari Nurul Khumaida Perkasa Arian Puji Lestari Rahadian Pratama Rahmawati, Fri Rava Raisha Putra Resti Rahmawati Putri Rini Kurniasih, Rini Roedhy Poerwanto Septiany C. Palilingan Sheryn Sunni Albani Siagian, Putri Junita Siregar, Josephine Elizabeth Siti Nurjanah Soekarno Mismana Putra Soekarno Mismana Putra, Soekarno Mismana Sogandi Sogandi Sogandi Sogandi Sudarsono Suharyanto Suharyanto Sulfianti, Asri Sulistiani sulistiani SURYANI Suryani Suryani Suryani Suryani Suryo Wiyono Sutoro Sutoro Syaeful Abidin Syamsul Falah Tatik Khusniati Tetty Chaidamsari Tetty Chaidamsari, Tetty Tri Panji Trini Suryani Kadir Vita Rosaline Fahri Waras Nurcholis Wasrin Syafii Wijiastuti Wijiastuti Yadi Suryadi Yahdiana Harahap Yulianto YUNITA ARIAN SANI ANWAR Zahra, Hafizh

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