Articles
            
            
            
            
            
                            
                    
                        Antibacterial Activity and Phytochemical Analysis of Geranium homeanum Turez Leaves 
                    
                    Fri Rahmawati; 
Maria Bintang; 
I Made Artika                    
                     Current Biochemistry Vol. 4 No. 3 (2017) 
                    
                    Publisher : IPB University 
                    
                         Show Abstract
                        | 
                             Download Original
                        
                        | 
                            
                                Original Source
                            
                        
                        | 
                            
                                Check in Google Scholar
                            
                        
                                                                    
                    
                        
                            
                            
                                
Geranium homeanum Turez is a herbaceous plant used as an empirical medicine. This research was carried out to test the antibacterial activity and determine minimum inhibition concentration (MIC) to Staphylococcus aureus and Pseudomonas aeruginosa with agar diffution method and phytochemical analysis of geranium leaves  by Harbone method. The young and old geranium leaves were blended then filtrated. The obtained filtrate was divided into two parts, one part heated by autoclave and the other was unheated. Each filtrate was tested against to Staphylococcus aureus and Pseudomonas aeruginosa. Geranium leaves filtrate having the highest antibacterial activity was heated at 500C until it  become dry powder.  The powder was used to measure MIC and phytochemical analysis.The results showed that the antibacterial activity of young leaves filtrate was higher than the old leaves filtrat, and the unheated leaves filtrate was higher than heated filtrate one. MIC of S. aureus and P. aeruginosa, were as follows 15 mg/ml and 20 mg/mL respectively. The antibacterial activity of powder geranium’s leaves  filtrate was weaker than 100 µg/mL ampicilline. Phytochemical analysis of geranium leaves showed positive contents of alkaloid and triterpenoid.
                            
                         
                     
                 
                
                            
                    
                        Pemanfaatan Bakteri Sebagai Pereduksi Emisi Gas Metana Pada Limbah Cair Kelapa Sawit (Elaeis guineesis Jacq.) 
                    
                    Nisa Widya Amanda; 
I Made Artika; 
Iman Rusmana                    
                     Current Biochemistry Vol. 4 No. 2 (2017) 
                    
                    Publisher : IPB University 
                    
                         Show Abstract
                        | 
                             Download Original
                        
                        | 
                            
                                Original Source
                            
                        
                        | 
                            
                                Check in Google Scholar
                            
                        
                                                                    
                    
                        
                            
                            
                                
Kelapa sawit merupakan salah satu tumbuhan penghasil minyak terbesar di Indonesia. Proses pengolahan buah kelapa sawit menjadi minyak memiliki dampak negatif, yakni terciptanya gas metana. Gas metana merupakan salah satu gas penyumbang efek rumah kaca yang menyebabkan pemanasan global. Oleh karena itu, diperlukan cara untuk menurunkan emisi gas metana. Tujuan penelitian ini adalah penggunaan bakteri untuk menurunkan emisi gas metana pada limbah cair pemrosesan buah kelapa sawit. Bakteri diisolasi dari limbah cair kelapa sawit. Terhadap isolat tunggal yang diperoleh dilakukan uji aktivitas enzim soluble methane monooxygenase (sMMO) dan particulate methane monooxygenase (pMMO). Isolat dengan aktivitas methane monooxygenase tertinggi dipilih untuk analisis sekuen DNA dan konstruksi pohon filogenetika. Tahap isolasi bakteri menghasilkan 13 isolat koloni tunggal. Uji aktivitas methane monooxygenase menunjukkan bahwa semua isolat tidak memiliki aktivitas sMMO. Sebaliknya, semua isolat memiliki aktivitas pMMO dengan tingkat berbeda yaitu dengan rentang nilai antara 0.10 – 0.22 M/mL kultur/hari. Analisis sekuen DNA menunjukkan bahwa isolat terpilih adalah Klebsiella sp. Berdasarkan uji Gram diketahui bahwa bakteri ini termasuk bakteri Gram negatif. Bakteri berpotensi digunakan untuk menurunkan emisi gas metan pada limbah cair pemrosesan buah kelapa sawit. Kata kunci: Klebsiella sp, 16S rRNA, Metana, pMMO, sMMO.
                            
                         
                     
                 
                
                            
                    
                        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                            
                                            
                    
                        
                            
                            
                                
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                            
                                            
                    
                        
                            
                            
                                
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                            
                                            
                    
                        
                            
                            
                                
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                            
                                            
                    
                        
                            
                            
                                
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                            
                                            
                    
                        
                            
                            
                                
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                            
                                            
                    
                        
                            
                            
                                
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                            
                                            
                    
                        
                            
                            
                                
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                            
                                            
                    
                        
                            
                            
                                
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.