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IWAN SASKIAWAN
Research Center for Biology, Indonesian Institute of Sciences
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Immunology & microbiology Medicine & Pharmacology

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Kajian Peningkatan Pati Resisten yang Terkandung dalam Bahan Pangan Sebagai Sumber Prebiotik Raden Haryo Bimo Setiarto; Betty Sri Laksmi Jenie; Didah Nur Faridah; Iwan Saskiawan
Jurnal Ilmu Pertanian Indonesia Vol. 20 No. 3 (2015): Jurnal Ilmu Pertanian Indonesia
Publisher : Institut Pertanian Bogor

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1093.301 KB) | DOI: 10.18343/jipi.20.3.191

Abstract

Prebiotics are food ingredients that selectively stimulate the growth of probiotic bacteria in the colon. Resistant starch (RS) is the starch that can not be digested by digestive enzymes and resistant to gastric acid so it can reach the colon to be fermented by probiotic bacteria. There are treatments to increase the content of RS such as: autoclaving-cooling cycling, combination of lintnerized with autoclaving-cooling, and combination of debranching pullulanase with autoclaving-cooling. The results of techno-economical study showed that the combination of fermentation followed by autoclaving-cooling can be used as an alternative technique to increase the content of resistant starch in food more effectively and efficiently.
Multiplex PCR for Rapid Detection of Rifampin and Isoniazid Resistance in Mycobacterium tuberculosis Isolated from Bandung, Indonesia IWAN SASKIAWAN; NUR HASANAH
Microbiology Indonesia Vol. 1 No. 3 (2007): December 2007
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5454/mi.1.3.4

Abstract

Mycobacterium tuberculosis resistant to rifampin and isoniazid, known as multidrug-resistant M. tuberculosis (MDR-TB) strains, is an emerging problem of great importance to public health, with higher mortality rates than for drug-sensitive strains. Rifampin resistance is due to mutations on the hot spot region of the rpoB gene, especially at positions 526 and 531, and isoniazid resistance is due to mutation on katG at position 315. Mechanisms of resistance are an appropriate target for molecular genotyping diagnostic methods. Here we examined the multiplex PCR assays for the rapid detection targeting rpoB526, rpoB531, and katG mutations. Sixty-one M. tuberculosis strains were studied based on rpoB526, rpoB531, and katG315 assays employing multiplex PCR. Of the 61 strains, the susceptibility tests determined 42 isolates were MDR-TB strains, 10, 4, and 5 isolates were resistant to rifampin, isoniazid, and at least to six drugs which prescibed for TB, respectively. The mutation profiles of the 42 MDR strains assayed by multiplex PCR were 81 and 38.1% on rpoB and katG, respectively. Six rifampin-resistant isolates (60%) had a mutation on rpoB, 25% isoniazid-resistant isolates had mutation on katG, and 20% of the isolates that were sensitive to all drugs tested had a mutation on rpoB. Sequencing analysis revealed sensitivity of the multiplex PCR assay for rpoB was 98.4% and was 100% for katG. There was a 19% difference between phenotype and genotype properties of all isolates detected. In conclusion, the sensitivity of multiplex PCR method was sufficient for preliminary detection of rpoB and katG mutations, but resistance M. tuberculosis to rifampin and isoniazid were not always conferred by mutated alleles on rpoB and, especially, on katG.
Biosynthesis of Polyamide 4, a Biobased and Biodegradable Polymer IWAN SASKIAWAN
Microbiology Indonesia Vol. 2 No. 3 (2008): December 2008
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (208.291 KB) | DOI: 10.5454/mi.2.3.5

Abstract

Polyamide 4, which is composed of repeating unit of g-aminobutyric acid (GABA), is a biobased and biodegradable polymer since it can be synthesized from renewable material instead of fossil-based material. GABA is produced by decarboxylation of glutamate (Glu) using glutamate decarboxylase (GAD: EC 4.1.1.15), which is produced by some microorganisms. In this study, enzymatic conversion of GABA from glutamate by Lactococcus lactis and Escherichia coli cell and chemical polymerization of GABA to polyamide 4 were revealed. The results show that GAD activity of E. coli was higher than that of L. lactis. The treatment of E. coli cell by heating and sonication increased the GAD activity and conversion rate of glutamate to GABA was up to 70.5%. The optimum temperature for this conversion is 37ºC. On the other hand, chemical synthesis of polyamide 4 was catalyzed by heating GABA at 215ºC for 2 minutes
Screening, Purification, and Characterization of Cellulase from Fungi Isolated from Used Mushroom Substrate IWAN SASKIAWAN; NUR HASANAH
Microbiology Indonesia Vol. 9 No. 4 (2015): December 2015
Publisher : Indonesian Society for microbiology

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (834.134 KB) | DOI: 10.5454/mi.9.4.5

Abstract

Alarge number of microorganism especially filamentous fungi has ability to degrade cellulose. The purpose of this study was to conduct screening, purification, and characterization of cellulase from fungi which was isolated from used paddy straw mushroom substrate. Screening of cellulytic activity using CMC medium shown that 11 out of 20 isolates of fungi produced a clearing zone surrounding fungal colony. Among them isolate number JMF 12 showed the highest cellulase activity and was further used for purification and characterization. The cellulase was purified to electrophoretical homogeneity by ammonium sulfate precipitation, dialyzed by Novagen D-Maxi TubeTM Dialyzer, and Sephadex G-100 gel filtration chromatography. The recovery and purification fold was 3.82 % and 1.98 respectively, after Sephadex G-100 gel filtration chromatograph. The o purified cellulase had an optimal pH and temperature at 6 and 45 C. The Km and Vmax of cellulase was 11.43 mM and 0.006mmol/min respectively. The purified cellulase was activated by Na+ and Zn++ but inhibited by Ca++, Co++, Fe++, and  Hg++ .
Co-Authors Betty Sri Laksmi Jenie Didah Nur Faridah NUR HASANAH Raden Haryo Bimo Setiarto