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INDONESIA
ANNALES BOGORIENSES
ISSN : 05178452     EISSN : 24077518     DOI : -
The Annales Bogorienses (ISSN: 0517-8452, E-ISSN: 2407-7518) is a peer-reviewed Journal that is published biannually. First published in 1955, it is now one of the oldest scientific journal in the nation. The Annales Bogorienses publishes original articles in basic and applied research as well as critical reviews and short communication in the fields of life sciences with the emphasis in biotechnology, molecular biology, and biochemistry.
Arjuna Subject : -
Articles 239 Documents
Partial Purification, Characterization, and Application of Extracellular Aspartic Protease from Lactobacillus casei WSP in Producing the Bioactive Peptides with Antibacterial and Antioxidant Activity Solikhin, Akhmad; Mustopa, Apon Zaenal; Suharsono, Suharsono; Putranto, Wendry Setiyadi
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2018.v22.n2.47-56

Abstract

   Lactobacillus casei WSP-derived an aspartic protease was sequentially purified by using chromatography gel filtration sephadex G-50. It resulted in a 22.81-fold increase of specific activity (51.5 U/mg) with a final yield of 1.9%. The estimated molecular weight of the purified enzyme was 37 kDa and showed gelatinolytic activity in zymogram assay. The enzyme exhibited optimum activity at 40ºC and pH 6 with casein as the substrate. Enzyme activity was significantly inhibited by pepstatin A (0.5 mM and 1 mM), confirming that this enzyme is a group of aspartic proteases, while other inhibitors such as EDTA, PMSF and iodoacetic acid showed no inhibition effect on the activity of enzyme. The addition of metal ion to the enzyme decreased enzyme activity, indicating the proteolytic enzyme was metal ion- dependent. Denaturant such as DDT tended to increase caseinolytic activity. Furthermore, this enzyme was capable of generating the new peptides from skimmed milk with the size 8 kDa, 10 kDa and 15 kDa. These peptides have potential as antibacterial and antioxidant agents.
Editor's Preface AB Vol 22 No 2 (2018) Rahmawati, Syamsidah
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (8.107 KB) | DOI: 10.14203/ann.bogor.2018.v22.n2.%p

Abstract

Non Invasive Detection of Dengue Viruses from Saliva: In vitro Study Saksono, Budi
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (214.71 KB) | DOI: 10.14203/ann.bogor.2018.v22.n2.75-80

Abstract

      In the previous paper, we had succeeded in developing an early detection system of dengue viruses using Sugar liganded Gold Nano Particle (SGNP) only from 6 μL serum. It has been reported that dengue virus is also detected in the saliva and urine of the patient. The evidences lead to the possibility of developing non-invasive methods of dengue virus detection. In this in vitro study, we evaluated the utility of SGNP to capture and concentrate dengue virion in 10% saliva solution. The results showed that dengue virion was successfully detected in 10% of saliva solution. Analysis of virion stability during storage showed that virions in salivary samples were stable up to 3 days at temperature wherease the RNA has significantly degraded. Although still a preliminary study, the data obtained show the prospect of SGNP as a non-invasive dengue virus detection method, as well as the development of POC (Point of Care) method. Clinical trials using saliva from dengue viruses infected patients need to be done to prove the effectiveness of the SGNP method.
Amelioration of Salt Tolerance in Soybean (Glycine Max. L) by Plant-Growth Promoting Endophytic Bacteria Produce 1-Aminocyclopropane-1-Carboxylase Deaminase Simarmata, Rumella; Ngadiman, Ngadiman; Rohman, Saifur; Simanjuntak, Partomuan
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (367.962 KB) | DOI: 10.14203/ann.bogor.2018.v22.n2.81-93

Abstract

     Salinity is a major abiotic stress that can induce ethylene synthesis beyond the normal limits as plants response to stress and hence reduces crop productivity. The 1-aminocyclopropane-1-carboxylase deaminase (ACCD)-producing bacteria can reduce excessive ethylene synthesis by taking ACC (ethylene precursor) as a nitrogen source. This study showed the possibility of using endophytic bacteria in order to reduce the undesirable effects of salinity. Strain Pseudomonas putida PIR3C and Roultella terrigena PCM8 exhibited promising performance for promoting the growth of plant under salinity stress conditions. The results showed that bacterial inoculation was effective even in the presence of higher salinity levels. Strain P. putida PIR3C was the most efficient strain compared to the other strains and significantly increased shoot length, root length, dry weight, germination percentage, and reduced stem diameter. The role of ACCD in reducing ethylene production under salinity stress conditions was also studied by measuring the evolution of ethylene in vitro by soybean seeds treated with some ACCD bacterial strain. The maximum ethylene lowering capacity was observed in R. terrigena PCM8, the strain reduced ethylene production from 622.81 nmol.g-1(control) to 352.78 nmol.g-1 (43% reduction). The production of α-ketobutyrate, chlorophyll content and germination percentage from P. putida PIR3C was higher than other strains. The results suggested that strain P. putida PIR3C and R. terrigena PCM8 can be employed for salinity tolerance in soybean seedlings and may have better prospects for an amelioration of stress condition.
Front Cover AB Vol 22 No 2 (2018) Rahmawati, Syamsidah
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (144.918 KB) | DOI: 10.14203/ann.bogor.2018.v22.n2.%p

Abstract

Optimization of Expression Condition, Two Dimensional And Melting Point-Based Characterization of Recombinant Human Interferon Alpha-2a Fusion and Non Fusion Forms Ningrum, Ratih Asmana; Wardhani, Widdya Kusuma; Wahyuni, Ike; Mustopa, Apon Zaenal
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1526.007 KB) | DOI: 10.14203/ann.bogor.2018.v22.n2.57-64

Abstract

     Recombinant Human Interferon Alpha-2a (rhIFNα-2a) is a therapeutic protein that used in hepatitis and cancer treatments. In our previous research, we developed higher molecular weight of the protein through human serum albumin fusion. The fusion and non fusion form of rhIFNα-2a were produced in Pichia pastoriswith 86 kDa and 19 kDa in size respectively. In previous research, protein yield was not reproducible due to unoptimized expression conditions. This reseach was aimed to optimize expression condition process and to characterize the fusion and non fusion forms of rhIFNα-2a. The parameters to observe in overproduction include nutrient (media and methanol concentration) and non nutrient (temperature andincubation period). Affinity and size exclusion cromatographicwere compared in protein purification. BCA assay was used to determine quantity of protein. Protein characterization was conducted using two-dimensional SDS PAGE and denaturation analyses. The optimal condition of expression was achieved using complex media with 1% of methanol for 3 day incubation period at 25°C. The protein yield was reproducible and higher comparing to previous research. Affinity chromatography resulted in higher purity of the proteins comparing to size exclusions. Characterization using two dimensional gel analysis revealed that isoelectric point of rhIFNα-2a is 6.5 for fusion form and 6.0 for non fusion form. The melting points of fusion protein were 56°C and 62°C whilst that of non fusion was 56°C.
Molecular Evaluation for Drought Tolerant Using Marker Assisted Breeding Method Fatimah, Fatimah; Prasetiyono, Joko; Trijatmiko, Kurniawan Rudi; Sustiprijatno, Sustiprijatno
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (425.55 KB) | DOI: 10.14203/ann.bogor.2018.v22.n2.94-100

Abstract

   The sustainability and increasing the national rice production require the readiness of food and agriculture sector cope with the impacts of climate change, land degradation, drought area, sloping production and the raising of population growth. Adaptation plays an important role in ensuring the sustainability of food security. This research aimed to develop drought-tolerant variety of Inpari 30 (submergence tolerance variety) and Situ Bagendit through marker-assisted backcrossing-through pyramiding gene of identified QTLs for foreground selection and to explore SSRs and 6K SNPs for background selection distributed in 12 rice chromosome of drought tolerant donor (Cabacu) and recipient rice (Inpari 30 and Situ Bagendit). The foreground selection revealed that flanking SSRs of each QTLs (qRPF2.1, qGPP2.1, qSPP4.1 and Sub1) was less than 2 cM. The background selection through polymorphic survey of Rice 6K SNP primers revealed 2457 (53,3%) polymorphic SNPs on Inpari 30 vs Cabacu and 2563 (55,6%) polymorphic SNPs on Situ Bagendit vs Cabacu with the average distance about 0.74 cM/chromosome. The genotypic selection of F1 Inpari 30/Cabacu and F1 Situ Bagendit/Cabacu have already in heterozygote condition for these 4 QTLs target. These lines was continued for backcross breeding to develop BC1F1 Inpari 30/Cabacu and BC1F1 Situ Bagendit/Cabacu generation.
Editorial Boards AB Vol 22 No 2 (2018) Rahmawati, Syamsidah
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (20.69 KB) | DOI: 10.14203/ann.bogor.2018.v22.n2.%p

Abstract

Guide for Authors AB Vol 22 No 2 (2018) Rahmawati, Syamsidah
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (24.663 KB) | DOI: 10.14203/ann.bogor.2018.v22.n2.%p

Abstract

Construction of pY-Af Vector for Expression of Thermostable α-L-Arabinofuranosidase in Saccharomyces cerevisiae Wirajana, I Nengah; Puspaningsih, Ni Nyoman Tri; Wasito, Eddy Bagus; Kusuma, Soekry Erfan; Kimura, Tetsuya; Sakka, Kazuo
ANNALES BOGORIENSES Vol 14, No 2 (2010): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (822.516 KB) | DOI: 10.1234/51

Abstract

In this research,  construction  of expression  vector  for thermostable α -L-arabinofuranosidase  in Saccharomyces cerevisiae was conducted. BJ1824 was conducted The  Escherichia coli/S. cerevisiae  shuttle vector, pYES2 was  used  as  parental  vector  in  construction.  The  abfA  gene  encoding  α-L- arabinofuranosidase  from Geobacillus  thermoleovorans  IT-08  was  amplified  by  PCR,  in  which  the  plasmid  pTP510 was  used  as  a template. The amplification product was treated with  SacI and XhoI and then subcloned to the pYES2 vector, which was previously digested with  SacI and  XhoI. The recombinant plasmid was designated as pY-Af and propagated  first  in  E.  coli  Top 10,  and  then  transformed  into  S.  cerevisiae  BJ1824.  For  α- Larabinofuranosidase (AbfA) production, the yeast transformants were grown in YNBG selective medium and YPG rich medium, using galactose as an inducer. The AbfA activity was assayed by measuring the amount of p-nitrophenol (pNP) released  from  p-nitrophenyl-α-L-arabinofuranoside  (pNPA) substrate at pH 6.0 and 70 C  for  30  min.  The  recombinant  AbfA  activity  was  detected  in  either  of  culture  medium  (0.98%),  cellassociated (14.17%) and intracellular (84.85%) when recombinant yeast was grown in YPG rich medium.Key words: α-L-arabinofuranosidase; Saccharomyces cerevisiae; expression vector

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