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Kusharyoto, Wien
Research Center for Biology-Indonesian Institute of Sciences
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Computer Science & IT

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AKTIVITAS ANTIBAKTERI AKTINOMISETES LAUT DARI PULAU ENGGANO [Antibacterial activity of marine actinomycetes from Enggano Island] Ratnakomala, Shanti; Apriliana, Pamella; Fahrurrozi, Fahrurrozi; Lisdiyanti, Puspita; Kusharyoto, Wien
BERITA BIOLOGI Vol 15, No 3 (2016)
Publisher : Research Center for Biology-Indonesian Institute of Sciences

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (3376.649 KB) | DOI: 10.14203/beritabiologi.v15i3.2258

Abstract

Marine actinomycetes were isolated from mangrove sediment from the coast in Enggano, Bengkulu Province, Indonesia using the medium NBRC No. 802 modified by the addition of 2% NaCl. A total of 29 isolates of actinomycetes were isolated from three mangrove sediment samples and evaluated their potential to produce bioactive metabolites. Screening of 29 isolates marine actinomycetes isolates were performed against three bacterial pathogens had been done. Bacteria test used was Escherichia coli NBRC 14 237, Staphylococcus aureus NBRC13 276, and Bacillus subtilis NBRC 3134. Screening result showed that seven isolates have inhibitory effects against bacteria test and 22 other isolates have no inhibition. Of the seven isolates, one isolate has inhibitory effect against the growth of Gram-negative bacteria Escherichia coli, while six other isolates inhibit Gram-positive bacteria Bacillus subtilis and Staphilococcus aureus. It was concluded that, of the 29 isolates conducted in the experiment, seven isolates produce antibacterial compounds on agar medium. Molecular identification of 23 isolates were identified based on  the gene 16S RNA sequences showed that 22 isolates belong to the genus Streptomyces and one strain belongs to the genus Dermacoccus.
VARIATION IN POINT MUTATIONS OF L -ARABINOSE ISOMERASE Thermotoga thermarum (TTAI) THROUGH THE ANALYSIS OF ENZYME STRUCTURE AND DOCKING SIMULATION Syahputra, Gita; Kusharyoto, Wien
Teknologi Indonesia Vol 40, No 1 (2017)
Publisher : LIPI Press

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Abstract

D-tagatose is one of the products of L-arabinose isomerase which can be applied to food, cosmetics, and health. D-tagatose produced by L-AI has a low quantity. L-AI enzyme from thermophilic bacteria as Thermotoga thermarum (TTAI) can produce higher quantity of D-tagatose than mesophilic bacteria. Point mutation can increase L-AI activity. The analysis of enzyme structure and docking simulation can determine the variation in point mutations. Based on analysis of enzyme structure and docking simulation, TTAI has 494 amino acids compiled by 17 of α-helix dan 18 of β-strand. The analysis of TTAI structure get several active side residues Gln16, Leu18, Tyr19, Phe81, Gln125, His126,Met183, Phe273, Glu300, Glu327, Tyr329, His344, Met345, Ile366, His442, His443. The docking simulation suggested that the residues for binding D-tagatose are Trp422 and Tyr331. Two point mutations, i.e. M183A and F273L, are recommended based on the analysis of TTAI structure, homology structure, residues, and docking simulation. This variation in mutation can be used for further research in vitro. 
STRUCTURAL CHARACTERIZATION OF FRACTIONATED GLYCOLIPID BIOSURFACTANTS SYNTHESIZED BY Pseudozyma aphidis YB205 Sari, Martha; Kartika, I Made; Kusharyoto, Wien
Teknologi Indonesia Vol 39, No 3 (2016)
Publisher : LIPI Press

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jti.v39i3.278

Abstract

Fractionation and structural characterization of glycolipid biosurfactant produced by yeast Pseudozyma aphidis strain YB205 was conducted. The yeast strain was grown in a nutrient broth with crude oil as the carbon sources and the glycolipid biosurfactant produced was isolated. The crude glycolipid was fractionated using column chromatography followed by complete separation and purification using extraction technique employing  different organic solvents. The fractions were subjected to activity test using oil displacement assay followed by chemical identity test using thin layer chromatography. In order to elucidate its chemical structure, the most active fraction was subjected NMR and FTIR analysis. Results showed that six major fractions were generated all of which showed biosurfactant activity. Four fractions is fractions 2, 4, 5, and 6 showed glycolipid characteristics and fraction 6 showed the highest biosurfactant activity. Combination of NMR and FTIR spectroscopy spectra indicated that chemical structures of fraction 6 belonged to glycolipid species.
EXPRESSION OF THE FLUORESCENT PROTEIN MTURQUOISE2 IN THE PERIPLASM OF Escherichia coli Handayani, Ira; Kusharyoto, Wien
Teknologi Indonesia Vol 39, No 3 (2016)
Publisher : LIPI Press

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (16.054 KB) | DOI: 10.14203/jti.v39i3.288

Abstract

Many variants of cyan fluorescent protein (CFP) have been developed as fluorescent tags which are widely used as donors in Förster resonance energy transfer (FRET) experiments. Recent improvement of CFP variants resulted in mTurquoise2, a brighter variant with faster maturation, high photostability, longer mono-exponential lifetime and the highest quantum yield measured for a monomeric fluorescent protein. Here, the authors describe the expression of mTurquoise2 targeted for secretion via the general secretory (Sec) translocation pathway into the highly oxidizing periplasm of Escherichia coli. The use of signal peptide MPB*1, a modified signal sequence of maltose binding protein was investigated. The His6-tagged fluorescent protein was expressed in E. coli NiCo21(DE3) and purified by means of immobilized metal ion affinity chromatography (IMAC) on TALON™ matrix. In SDSPAGE and Western blot analysis, a single band corresponding to a molecular mass of approximately 28 kDa was observed, which correlated with the predicted molecular mass based on the amino acid sequence of mTurquoise2. 
Co-Authors Abd. Rasyid Syamsuri Apriliana, Pamella Gita Syahputra Handayani, Ira I Made Kartika Martha Sari PUSPITA LISDIYANTI SHANTI RATNAKOMALA