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Microbiology Indonesia

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Published by Perhimpunan Mikrobiologi Indonesia

ISSN : 19783477 EISSN : 20878575 DOI : -

Core Subject : Health, Science,

Biochemistry, Genetics & Molecular Biology Immunology & microbiology Medicine & Pharmacology

Microbiology Indonesia provides a unique venue for publishing original researches in microbiology (espesially from Indonesian reseachers), and ensures that authors could reach the widest possible audience. Microbiology Indonesia publishes a wide range of research disciplines on bacteria, archaea, fungi, protozoa, and virus as well as biotechnology related to microbiology. Topics include (but are not limited to): -methods in microbiology, -bioprocess, -environmental microbiology, -food microbiology, -plant-microbe interaction, -animal-microbe interactions, -microbial community, -microbial genetics, -virology, -comparative and functional microbial genomics, -and gene expression in microbes.

Arjuna Subject : Imunologi dan Mikrobiologi (semua kategori) - Mikrobiologi dan Bioteknologi Terapan

Articles 398 Documents

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Characterization and Phylogenetic Analysis of Soybean Rhizobial Strains from Java and Sumatra SETIYO HADI WALUYO
Microbiology Indonesia Vol. 5 No. 4 (2011): December 2011
Publisher : Indonesian Society for microbiology

Twenty-seven and twenty-four soybean rhizobial isolates from Java and Sumatra, respectively,were characterized. Based on cross-inoculation, eight isolates from Java and nine from Sumatra could be grouped as soybean specific rhizobial species , while 19 isolates from Java and 15 from Sumatra were promiscuous. ARDRA of intergenic spacer region of 16S-23S rDNA showed that the isolates from Java were different from those from Sumatra. Six soybean specific isolates from Java and one from Sumatra were in the same cluster with the reference strain, Bradyrhizobium japonicum USDA 110, thus could be classified as B. japonicum. One soybean specific isolate from Java’s has a distinct position, while the other soybean specific isolate from Java was placed in another group dominated by isolates from Sumatra. The nineteen promiscuous isolates from Java were clustered in a different group. This group, together with the isolate with distinct position and the other group that were dominated by isolates from Sumatra, were distinct from B. japonicum USDA 110. Therefore it is tempting to speculate that they represent indigenous soybean rhizobial strains. Based on complete sequencing of the amplified 16S rDNA of 21 selected isolates, these isolates could be divided into three groups consisting of twelve Bradyrhizobium elkanii, eight Bradyrizobium japonicum and one Sinorhizobium fredii. Most of the B. elkanii strains were isolated from acid soils at Sitiung, West-Sumatra, while only two isolates were obtained from Java. Four isolates from Java, two isolates from Sitiung, and two isolates from Bukit Tinggi were identified as B. japonicum. One isolate from Java with a distinct position on the ARDRA was identified as S. fredii.

Photosynthesis of Periphyton and Diffusion Process as Source of Oxygen in Rich-Riffle Upstream Waters NIKEN TUNJUNG MURTI PRATIWI; SIGID HARIYADI; RIFKI TAJUDIN
Microbiology Indonesia Vol. 5 No. 4 (2011): December 2011
Publisher : Indonesian Society for microbiology

Most of dissolved oxygen content in stream or river water is obtained from the process of photosynthesis and diffusion. Photosynthesis process in running water is performed by autotrophic organisms, especially community of attached micro-algae or periphytic micro-algae that live attached to stone or other substrates, while intensive diffusion process occurred as water flows. Rich riffle upstream waters are characterized by stony bottom and high current. The role of the periphyton photosynthesis result and diffusion process along the water current was examined by this research. A field experimental observation was carried out at the upstream of Cisadane River (600m asl) with two different natural light conditions, the light or exposed (24630-104240 Lux) and shadowy (11120-65300 Lux) conditions. The actual dissolved oxygen contents in the area with the two conditions are relatively similar; 7.3 (light) and 7.0 mg L-1 (shadowy). Oxygen supports were significantly different at the light and shadowy conditions, whether from diffusion process 71.71% and 79.37%, respectively, or from periphyton photosynthesis, 21.73% and 15.30%, respectively. The compositions of periphytons living in the two conditions were similar; mostly composed by group of Diatom, with the same dominant species of Thalassiothrix sp. The difference in periphyton growth was shown by its density. In the light condition, the Diatom tends to grow at higher density in comparison to the shadowy condition. The role of periphyton to support oxygen in upstream waters is light dependent. The higher the light intensity (Photosynthetic Active Radiation ranged), the higher the support of oxygen will be.

Selection of Carbon and Nitrogen Source for 8-Hydroxy 9, 12-Octadecadienoic Acid Production using Endophytic Fungi Curvularia lunata BioMCC FE-00283 ERWAHYUNI ENDANG PRABANDARI; TUN TEDJA IRAWADI; WAHONO SUMARYONO; KHASWAR SYAMSU
Microbiology Indonesia Vol. 5 No. 4 (2011): December 2011
Publisher : Indonesian Society for microbiology

Hydroxyoctadecadienoic acid (HODE) is one of hydroxy fatty acids that has anticancer activity. HODE was previously produced by chemical synthesis or bioconversion from linoleic acid. This is the first paper reported production of HODE by Curvularia lunata an endophytic fungi of Cibotium barometz. Various carbon and hydrogen sources have been tested for their effects on the production of HODE by C. lunata. Glucose, lactose, maltose, xylose, and sucrose were used as carbon sources, while yeast extract, monosodium glutamate, urea, and NH4Cl were used as nitrogen sources. Fermentation was done using 100 ml medium in 250 ml Erlenmeyer flask at 150 rpm, 28 oC for 10 days. HODE products were analyzed by high pressure liquid chromatography using C18 coloumn and eluted by gradient system of acetonitril-water from 15% to 100%. Glucose and monosodium glutamate were found to be the best carbon and nitrogen source. The optimum concentration of glucose and monosodium glutamate for the production of HODE were 10 mg L-1 and 12 mg L-1 respectively.

Cloning of α-L-arabinofuranosidase Genes and Its Expression in Escherichia coli: A Comparative Study of Recombinant Arabinofuranosidase Originatingin Bacillus subtilis DB104 and Newly Isolated Bacillus licheniformis CW1 MOCHAMAD NURCHOLIS; NIKNIK NURHAYATI; IS HELIANTI; MARIA ULFAH; BUDIASIH WAHYUNTARI; AGUSTIN KRISNA WARDANI
Microbiology Indonesia Vol. 6 No. 1 (2012): March 2012
Publisher : Indonesian Society for microbiology

Arabinofuranosidase (Abfa) is one of the most important enzymes involved in degradation of lignocelullose biomass. Two genes encoding α-L-Arabinofuranosidase (abfA), each from Bacillus subtilis DB104 (abfAa1) and an indigenous Indonesian B. licheniformis CW1 (abfAb3), were cloned by the PCR approach and expressed in Escherichia coli. Sequences analysis of abfAa1 and abfAb3 revealed that each consists of 1721 and 1739 base pairs long DNA, respectively. Each clone contains a hypothetical open reading frame of 1503 and 1509 bp that encode an Abfa protein of 500 and 502 amino acids for abfAa1 and abfAb3, respectively. The deduced amino acid sequence of AbfaB3 shares 75% identity to that of AbfaA1. The recombinant enzymes were expressed constitutively in E. coli. Partial characterization of those enzymes revealed that the AbfaA1 and AbfaB3 were optimally active at 50 ºC and 60 ºC at pH 6, respectively. Thermostability studies of the recombinant enzymes with p-nitrophenyl α-L-arabinofuranoside at their optimal conditions showed that up to 50% AbfaA1 activity was lost after 5 h incubation at 50 ºC, whereas the AbfaB3 retained its activity over 75% after 12 h pre-incubation oat 60 ºC. This thermostability study of recombinant AbfaB3 showed for the first time that the arabinofuranosidase from B. licheniformis is a thermostable enzyme. The recombinant enzyme showed a higher optimal reaction temperature (60 ºC) in comparison to the previously reported thermostable arabinofuranosidase. The thermostable AbfaB3 has a potential to be applied to the degradation of lignocellulose biomass synergistically with thermostable xylanases, for instance in the production of xylo-oligosaccharides.

The Effect of Growth Medium pH towards Trypsin-Like Activity Produced by Lactic Acid Bacteria DYAH WULANSARI; BUDIASIH WAHYUNTARI; TRISMILAH TRISMILAH; ASTUTIATI NURHASANAH
Microbiology Indonesia Vol. 6 No. 2 (2012): June 2012
Publisher : Indonesian Society for microbiology

In cases of pancreatic disease, trypsin deficiency often occurs due to reduced expression of trypsin in the pancreas. Patients with pancreatic problem can be treated with a supplement containing digestive enzymes, including trypsin. However, most of the enzymes currently used for the treatment are derived from porcine and bovine sources. On the other hand, lactic acid bacteria are also known to show trypsin-like activity. In the previous work, our group screened 11 lactic acid bacteria isolates, which had previously been proven to show serine protease activity, for trypsin-like activity. The strains were initially grown in MRS (de Mann, Rogosa and Sharpe) medium before being transferred directly to the production medium to produce trypsin. During the previous study, the initial pH of the production medium was set at 6 (the same as the MRS medium pH), which is the optimum pH for the cell growth of lactic acid bacteria. However, most trypsin has an optimum pH of around 8. In this study, we altered the production medium pH to 8 and we harvested the lactic acid bacteria from MRS medium by centrifugation prior to their inoculation to the production medium. Observation of the culture growth and enzyme activity indicated that the new strategy improved the enzyme activity expressed by some strains.

Application of Phenol Pretreatment for the Isolation of Rare Actinomycetes from Indonesian Soil YUDHIE ISTIANTO; RADEN SETYO ADJI KOESOEMOWIDODO; YOSHIO WATANABE; HARDANING PRANAMUDA; BAMBANG MARWOTO
Microbiology Indonesia Vol. 6 No. 1 (2012): March 2012
Publisher : Indonesian Society for microbiology

Phenol treatment was applied for isolation of rare Actinomycetes using 25 soil samples collected from Pulau Seribu, Tanjung Redep, Manokwari, and Halmahera. The samples were air-dried and suspended in 1.5 % (w/v) phenol solution at 30 oC for 30 minutes, and subsequently cultured on plates of humic acid-vitamin agar (HVA) medium supplemented with cycloheximide (50 μg/mL) and nystatin (50 μg/mL). A total of 61 isolates were obtained and the most dominant isolates were not Streptomyces (only 24.6%), whereas other genera such as Micromonospora, Actinomadura, Microbispora and Polymorphospora were isolated with ratios of 49.2%, 13.1%, 9.8%, and 3.3%, respectively.

Five Unique Amino Acid Residues of Hemagglutinin (HA) Proteins of Swine Influenza A (H1N1) Detected in 2009 in Jakarta, Indonesia ANDI YASMON; YULIANTY MUHAYAR; VIVI SETIAWATY; BETI ERNAWATI DEWI; BUDIMAN BELA; FERA IBRAHIM
Microbiology Indonesia Vol. 6 No. 2 (2012): June 2012
Publisher : Indonesian Society for microbiology

Nine HA genes of influenza A (H1N1) viruses originating from swine which were detected in 2009 in Jakarta, Indonesia, were characterized in this study. Nasopharyngeal and/or pharyngeal samples were extracted to obtain viral RNA genomes. Amplification of the HA segment was performed by using the reverse transcription-polymerase chain reaction (RT-PCR), and followed by nested PCR in cases of RT-PCR negative. DNA sequencing was performed by using eight overlapping primers. All the Jakarta strains were closely related to vaccine strain A/California/07/2009. Nine amino acid changes were found in the Jakarta strains, and 5 (P100S, S220T, G239D, R240Q, and I338V) of those were unique to all Jakarta strains with respect to strain A/California/07/2009 used to produce vaccine. An I338V substitution was detected in a cleavage site of HA and no amino acid changes were detected in potential sites for N-linked glycosylation. For seven sites (positions 131, 158, 160, 183, 187, 222, and 227) playing an important role in viral attachment to host receptor, none of the expected amino acid changes was detected; however, a S220T substitution close to amino acid 222 was found in all the Jakarta strains. All amino acid changes potentially affect the pathogenicity of the viruses and the efficacy of strain A/California/07/2009 in neutralizing the Jakarta strains.

Isolation and Identification of a Thermostable Amylase-Producing Bacterium from Hatuasa Hotspring DOMINGGUS MALLE; JUNUS PICARIMA; LAURY CHARA HUWAE; INDRA RAHMAWATI; WAHYU PURBOWASITO
Microbiology Indonesia Vol. 6 No. 2 (2012): June 2012
Publisher : Indonesian Society for microbiology

Hot springs are a common source of thermophyles which produce thermostable enzymes. The objective of this study was to isolate and identify thermostable amylase-producing bacteria from a local geothermal spring. An amylase–producing bacterium strain was isolated from this hot spring which excreted amylase after being grown on starch agar screening plates at 37 °C. It was identified as Bacillus megaterium using the method of 16S ribosomal DNA. The organism is a rod-shape and is a spore-forming bacterium. Maximum amylase production was achieved after incubation in the production media for 72 hours. Preliminary analysis of the secreted amylase showed that the enzyme could bind to DEAE-Sepharose matrix and was discharged by eluting with 0.5 M NaCl. The partially purified enzyme was stable up to 75 °C, showing that this enzyme might have potential application in the starch-processing industry.

Mercury (Hg)-Resistant Bacteria in Hg-Polluted Gold Mine Sites of Bandung, West Java Province, Indonesia SITI KHODIJAH CHAERUN; SAKINAH HASNI; EDY SANWANI; MAELITA RAMDANI MOEIS
Microbiology Indonesia Vol. 6 No. 2 (2012): June 2012
Publisher : Indonesian Society for microbiology

In the present study, ten mercury-resistant heterotrophic bacterial strains were isolated from mercurycontaminated gold mine sites in Bandung, West Java Province, Indonesia. The bacteria (designated strains SKCSH1- SKCSH10) were capable of growing well at ~200 ppm of HgCl except for strain SKCSH8, which was able to grow at 550 ppm HgCl . The bacteria were mesophylic and grew optimally at 1% NaCl at neutral pH with the optimal growth temperature of 25-37 ºC. Phenotypic characterization and phylogenetic analysis based on the 16S rRNA gene sequence indicated that the isolates were closely related to the family Xanthomonadaceae, Aeromonadaceae, and Pseudomonadaceae and they were identified as Pseudomonas spp., Stenotrophomonas sp., and Aeromonas sp. Eight bacterial strains were shown to belong to the Pseudomonas branch, one strain to the Stenotrophomonas branch and one strain to the Aeromonas branch of the ã-Proteobacteria. Phylogeny based on their 16S rRNA gene sequences indicated that four of the isolates (SKCSH1, SKCSH4, SKCSH7, SKCSH9) could be classified as representatives of four novel species in the genus Pseudomonas that were allocated to P. moraviensis (96.96% similarity) and P. plecogossicida (94.53, 96.61, and 96.73% similarity). Four other isolates could be allocated to P. plecogossicida (97.57 and 98.66% similarity) and P. hibiscicola (99.97% similarity), one isolate to Stenotrophomonas africana (99.69% similarity), and one other isolate to Aeromonas hydrophila subsp. ranae (99.43% similarity). The findings of this study provide the first information of the phylogenetically-diverse Hg-resistant bacteria in the Hg-polluted sites of Indonesia that may be highly useful for developing in situ bioremediation or detoxification of Hg-contaminated sites in Indonesia.

Properties of an Extracellular Protease of Bacillus megaterium DSM 319 as Depilating Aid of Hides BUDIASIH WAHYUNTARI; HENDRAWATI HENDRAWATI
Microbiology Indonesia Vol. 6 No. 2 (2012): June 2012
Publisher : Indonesian Society for microbiology

Properties of a Bacillus megaterium DSM319 extracellular protease which are related to its application for depilating hides were investigated. The properties observed were optimum temperature and pH, the type of protease, and type of the protein which could be hydrolyzed by the enzyme. The enzyme was produced in a 3.5 liters LKB jar fermentor in a medium containing (2.0% v v-1 molasses and 1.3% w v-1 urea at 37 ºC , pH 7.5, aeration 1 vvm, agitation 250 rpm for 24 hours). The enzyme solution was concentrated by means of membrane ultrafiltration followed by ammonium sulfate precipitation at 70% w v-1 saturation. Optimal temperature and pH were observed at 30 ºC and pH 8 respectively. Two mM PMSF and EDTA inhibited the enzyme leaving level of activity of 84.5 and 4.3% correspondingly, indicated that the crude enzyme might be a metal requiring serine protease. The presence of 0.5, 2.0, and 3.5 mM CaCl caused an increase of the enzyme activity of 73, 88, and 79% respectively. The enzyme was able to hydrolyze Na-Benzoyl-DL-Arginine p-Nitro Anilide, a specific amino acid sequence cleaved by trypsin at a reaction rate of 0.024 absorbance value at 405 nm per minute. The enzyme was capable of hydrolyzing bovine serum albumin, hemoglobin, and gelatin, and to hydrolyze alkaline soluble collagen and keratin. The K value of the enzyme for hydrolysis of bovine serum albumin and gelatin was 3.44 m and 1.65 mg mL-1, whereas V values were 8.09 and 55.24 mg mL-1 respectively. The experimental data showed max that the crude enzymes have potential for dehairing of cowhides.

Page 34 of 40 | Total Record : 398

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Iman Rusmana

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kPERHIMPUNAN MIKROBIOLOGI INDONESIA (SeKretariat PERMI), Gedung 10.2 Indonesian Life Sciences Center (ILSC), Zona Bisnis Teknologi Puspiptek, Jalan Raya Serpong - Bogor Gunung Sindur, Jawa Barat 16340, Indonesia. Email: microbiology.indonesia@gmail.com

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INDONESIA

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Home Page

OAI Link

Editorial Team

Contact

Reviewer

Google Scholar

Contact Name Iman Rusmana

Contact Email rusmana13@yahoo.com

Phone +62217560536

Journal Mail Official microbiology.indonesia@gmail.com

Editorial Address kPERHIMPUNAN MIKROBIOLOGI INDONESIA (SeKretariat PERMI), Gedung 10.2 Indonesian Life Sciences Center (ILSC), Zona Bisnis Teknologi Puspiptek, Jalan Raya Serpong - Bogor Gunung Sindur, Jawa Barat 16340, Indonesia. Email: microbiology.indonesia@gmail.com

Location Kota tangerang, Banten INDONESIA

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Abstract

Contact Name
Iman Rusmana

Contact Email
rusmana13@yahoo.com

Phone
+62217560536

Journal Mail Official
microbiology.indonesia@gmail.com

Editorial Address
kPERHIMPUNAN MIKROBIOLOGI INDONESIA (SeKretariat PERMI), Gedung 10.2 Indonesian Life Sciences Center (ILSC), Zona Bisnis Teknologi Puspiptek, Jalan Raya Serpong - Bogor Gunung Sindur, Jawa Barat 16340, Indonesia. Email: microbiology.indonesia@gmail.com

Location
Kota tangerang,

Banten

INDONESIA