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Antibacterial Activity of Leaf Extracts of Anredera cordifolia (Ten.) Steenis and Muntingia calabura L. Against Streptococcus pneumoniae Nuke Annisa Nasution; I Made Artika; Dodi Safari
Current Biochemistry Vol. 7 No. 1 (2020)
Publisher : IPB University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.29244/cb.7.1.1

Abstract

Antibacterial resistance in Streptococcus pneumoniae has been increasing and is one of ongoing global concern. The need to find new antibacterial agents against Streptococcus pneumoniae is of paramount importance. Medicinal plants are prospective sources of antibacterial agents. The aims of the present study were to determine the activity of leaf extraxt of Anredera cordifolia (Ten.) Steenis and Muntingia calabura L. against Streptococcus pneumoniae. Leaves of Anredera cordifolia (Ten.) Steenis were extracted using 96% ethanol, while the leaves of Muntingia calabura L were extracted using 100% methanol. The leaf extracts of the two plants obtained were bioassayed for antibacterial activity against Streptococcus pneumoniae ATCC 49619 and a clinical isolate Streptococcus pneumoniae PU 067. Results showed that leaf extracts of both Anredera cordifolia (Ten.) Steenis and Muntingia calabura L. have antibacterial activity in vitro against Streptococcus pneumoniae ATCC 49619 at crude extract concentrations of 25%, 50%, 75% and 100% (w/v). Both plants extracts showed strongest activity against S. pneumoniae ATCC 49619 at extract concentration of 75%. In addition, the extracts of both plants have inhibitory activity against growth of the clinical isolate Streptococcus pneumoniae PU 067. Both plant extracts showed strongest activity against S. pneumoniae PU 067 at extract concentration of 100%. Therefore, leaf extracts of Anredera cordifolia (Ten.) Steenis and Muntingia calabura L. can potentially be used as a source of antibacterial agent for Streptococcus pneumoniae. Keywords: Antibacterial agent, Anredera cordifolia (Ten.) Steenis, Muntingia calabura L., Streptococcus pneumoniae.
Minimum Concentration of Stingless Bee Propolis (Trigona sp.) in Inhibiting the Growth of Dandruff Bacteria Akhmad Endang Zainal Hasan; I Made Artika; Erlank Bagjavicenna
Current Biochemistry Vol. 8 No. 1 (2021)
Publisher : IPB University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.29244/cb.8.1.2

Abstract

Lack of confidence in men and women, one of which is when there is dandruff on the hair and scalp. Hair loss is a further symptom of the presence of white scales on the scalp that cause itching. The presence of excessive microorganisms can aggravate this dandruff. Ingredients such as ketocanozole, zinc pyrithione, selenium sulfide and sulfur are compounds commonly used in shampoo formulas. Propolis is an alternative natural ingredient to treat dandruff. The purpose of this study was to determine the minimum growth inhibitory concentration (MIC) of propolis against dandruff-causing bacteria. Dandruff-causing microbes were isolated from dandruff hair and with the well method in a petri dish, the minimum growth inhibitory concentration of propolis was determined. The microbial colonies produced were very diverse with a round shape like grapes, yellowish white in color. The concentration of 6.25% is the MIC value of propolis extract against dandruff microbes. The effectiveness values against ketoconazole and propolis X from the tested propolis extract were 223.52% and 99.59%, respectively. Keywords: hair loss, dandruff, propolis, bacteria , Trigona
Analysis and Prediction of some Histone-derived Antimicrobial Peptides from Toads Duttaphrynus melanostictus and Phyrinoidis asper Muhammad Dailami; I Made Artika; Mirza Dikari Kusrini
The Journal of Pure and Applied Chemistry Research Vol 5, No 2 (2016)
Publisher : Chemistry Department, The University of Brawijaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1579.558 KB) | DOI: 10.21776/ub.jpacr.2016.005.02.231

Abstract

Antimicrobial peptides in skin secretions of toads is a promising methods to combat a wide spectrum of bacteria. Histone H2A is a type of DNA-binding protein that acts as a precursor for several antimicrobial peptides. In toads (family Bufonidae) buforin I and buforin II are examples of antimicrobial peptides that derived from histone H2A. This study investigated the genetic diversity and phylogenetic analysis and in silico prediction of antimicrobial peptides derived from histone H2A of Duttaphrynus melanostictus and Phyrinoidis asper, which were collected from Bogor Agricultural University’s campus area. A new set of primers (Buf_fwd and Buf_rev) were designed by using PrimerBLAST, to amplify 393 nucleotides of the histone H2A gene that codes 131 amino acids. Haplotype diversity of both species are very low. Phylogenetic analysis shows the sample D. melanostictus and P. asper are separated to each other in two different clades. Several short predicted peptides from histone H2A show a potential as an antimicrobial peptides based on in silico prediction. Psychochemical characteristics and 3D structure of potent antimicrobial peptides are described.
The characterization of bacteriocins produced by Lactobacillus plantarum strains isolated from traditional fermented foods in Indonesia and the detection of its plantaricin-encoding genes Sogandi Sogandi; Apon Zaenal Mustopa; I Made Artika
Indonesian Journal of Biotechnology Vol 24, No 1 (2019)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (22.128 KB) | DOI: 10.22146/ijbiotech.42582

Abstract

Lactobacillus plantarum is widely found in either anaerobic plant matter or fermented foods, and it has been recognized as producing antimicrobial bacteriocins. This study aimed to characterize the antimicrobial bacteriocins of L. plantarum and detect its genes that encode plantaricins. Samples were isolated from traditional fermented foods from Indonesia. Antimicrobial activity was evaluated using the agar diffusion assay procedure. The titration method applied the maximum amounts of lactic acid at 1054 mg/mL and hydrogen peroxide at 3.85 mg/mL. Based on the results, the supernatant of the L. plantarum strains appeared to have a broad spectrum of antimicrobial activity against pathogens, which would be active at pH 2.0–12.0 and stable temperature. In addition, almost all of the L. plantarum strains contained plantaricin-encoding genes (e.g. plnA, plnF,plnJK, and plnW), which were grouped into one cluster as indicated by phylogenetic analysis. Therefore, this study discovered clear evidence of the potential of some L. plantarum strains to act as antimicrobial agents.
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

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (184.253 KB) | DOI: 10.5454/mi.1.1.8

Abstract

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

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (56.212 KB) | DOI: 10.5454/mi.1.2.9

Abstract

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

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (110.003 KB) | DOI: 10.5454/mi.3.1.7

Abstract

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

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (72.414 KB) | DOI: 10.5454/mi.4.3.%p

Abstract

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

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (73.696 KB) | DOI: 10.5454/mi.5.3.1

Abstract

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.
CAMPURAN PROPOLIS DAN GARAM KELAPA SEBAGAI BAHAN ANTIBAKTERI PLAK GIGI MIXED PROPOLIS AND COCONUT SALT AS A DENTAL PLAQUE ANTIBACTERIAL AGENT Akhmad Endang Zainal Hasan; I Made Artika, Henry Adiprabowo
FITOFARMAKA: Jurnal Ilmiah Farmasi Vol 2, No 2 (2012): FITOFARMAKA
Publisher : Universitas Pakuan

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (402.064 KB) | DOI: 10.33751/jf.v2i2.168

Abstract

Karies gigi merupakan masalah kesehatan yang umum terjadi di kalanganmasyarakat Indonesia. Faktor yang paling banyak menyebabkan karies gigi adalah plak gigi.Bakteri yang dominan dalam plak gigi adalah Streptococcus mutans. Salah satu bahanantibakteri kariogenik yang biasa dipakai dalam pasta gigi saat ini adalah fluor. Penggunaanpasta gigi berfluor dapat menimbulkan fluorosis yaitu pelemahan email gigi bila dipakaidalam konsentrasi yang berlebihan. Propolis dan garam kelapa merupakan bahan alamiyang berpotensi sebagai antibakteri pengganti fluor. Penelitian bertujuan untuk mengujiaktivitas antibakteri dari campuran propolis dan garam kelapa dan membandingkankeefektifannya dengan antibakteri NaF yang terdapat dalam pasta gigi komersial. Ujiaktivitas antibakteri S. mutans dilakukan dengan metode hitungan cawan yaitupenghitungan jumlah bakteri yang tumbuh di media contoh dalam cawan petri. Propoliskasar diekstrak dengan alkohol dan didapatkan rendemen sebesar 8.52%. Hasil penelitianmenunjukkan bahwa campuran propolis 6.25% dan garam kelapa 1 M mempunyaikemampuan paling besar sebagai antibakteri dan dapat menghambat S. mutans lebih baikdaripada NaF 0.3%. Keefektifan propolis-garam terhadap NaF 0.3% sebesar 203.88%.Kata kunci : propolis, garam kelapa, antibakteri, antikaries gigi, Streptococcus mutans,
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 Dhani Luthfi Ramadhani 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 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