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Articles by Dessy Natalia
Total Records ( 4 ) for Dessy Natalia
  Zeily Nurachman , Sari Dewi Kurniasih , Ferra Puspitawati , Sarwono Hadi , Ocky Karna Radjasa and Dessy Natalia
  Problem statement: An Indonesian marine bacterial isolate, Bacillus amyloliquefaciens PSM 3.1 was isolated for hydrolyzing cellulose. A 1500-bp nucleotide fragment was amplified from the chromosomal DNA by the use of primers directed against the conserved sequence of Bacilli endoglucanase genes obtained from GenBank. Approach: The fragment was cloned and expressed in Escherichia coli. Results: The endoglucanase gene (eglII gene) had an open reading frame of 1500 nucleotides encoding a protein of 499 amino acids. The EglII protein belonged to Glycosyl Hydrolase family 5 (GH5) with a Cellulose Binding Module 3 (CBM 3). The structure model of the EglII protein revealed that the catalytic residues seemed to be Glu169 (as proton donor) and Glu257 (as nucleophile) and the catalytic triad residues were Thr256, His229 and Glu169. The EglII endoglucanase exhibited an optimum pH of 6.0 and temperature of 50°C and the enzyme tolerated to high salt concentration. Conclusion/Recommendations: This EglII endoglucanase is a promising candidate for many applications in biomass degradation.
  Zeily Nurachman , Alfredo Kono , Ocky Karna Radjasa and Dessy Natalia
  Problem statement: Bacteria from the surface of the tropical marine hard coral Acropora sp. were screened for producing raw-starch-degrading-α-amylase. Approach: Based on its 16s rDNA sequence, a bacterium that produced the highest amylolitic activity was identified as Bacillus amyloliquifaciens ABBD. The bacterial isolate secreted a α-amylase extracellularly and then the enzyme was partially purified by ammonium sulfate precipitation followed by anion exchange chromatography. Results: Electrophoresis results both SDS-PAGE and native PAGE suggested that the enzyme was a heterodimeric protein (97 kDa) consisting of 45 and 55 kDa subunits. The α-amylase had an optimum pH of 7.0 and temperature of 60°C. More than 80% activity of the enzyme was retained under high salt conditions (up to 20% NaCl). The enzyme remained stable at 50°C for 1 h. Starch hydrolysis by the enzyme at 70°C yielded oligosaccharides (G2-G4) and at room temperature yielded glucose/maltose (G1 and G2). Conclusion: The B. amyloliquifaciens ABBD α-amylase was capable of degrading various raw starch granules from corn, rice, cassava and sago at room temperature.
  Ernawati Arifin Giri- Rachman , Indah Woro Utami , Shinta Kusumawardani , Debbie Soefie Retnoningrum , Dessy Natalia , Nurfitriani , Gilang Nadia , Patricia Gita Naully and Neni Nurainy
  Hepatitis B is the most common liver infection worldwide. The recombinant Virus Like Particles (VLP) of small Hepatitis B surface antigen (s-HBsAg) vaccine provides excellent protection against Hepatitis B Virus (HBV). In this study, we have generated a construct of Pichia pastoris recombinant which comprises multi expression cassettes encoding s-HBsAg which belongs to HBV B3 genotype predominantly found in Indonesia. An expression cassette containing a synthetic codon optimized open reading frame of HBV B3 genotype/adw serotype s-HBsAg was cloned into pAO815 to generate pAOHBs1 in Escherichia coli. The expression cassette from pAOHBs1 was subsequently isolated and ligated with recombinant previously obtained, generated recombinant plasmid containing 2, 3 and 4 direct repeats of HBsAg expression cassette. The resulted recombinant containing 4 expression cassettes was integrated to P. pastoris genome. Positive integrants and stability during cultivation were identified by PCR and qPCR. The expression of s-HBsAg was induced by methanol and analyzed by SDS PAGE and western blotting. Nucleotide sequencing analysis showed that the inserted fragment encodes amino acids with 100% similarity compared to that designed for HBV B3 genotype. The PCR and qPCR analysis showed that stable P. pastoris integrated with 4 s-HBsAg expression cassette was successfully obtained with methanol utilizing slow phenotype. A protein band with apparent molecular weight which similar to s-HBsAg size was detected based on a SDS PAGE and western blot analysis. A stable integrant of P. pastoris containing four expression cassettes of HBV B3 genotype s-HBsAg capable of producing a vaccine candidate against Hepatitis B was generated.
  Minda Azhar , Dessy Natalia , Sumaryati Syukur , Vovien and Jamsari
  Fructose and Fructo-Oligosaccharides (FOS) are derived more practical from the enzymatic hydrolysis reaction of inulin. In this study, the gene fragments that encodes inulin hydrolysis enzyme were isolated from genomic B. licheniformis by Polymerase Chain Reaction (PCR) technique using new primers designed on conserved domain in family GH32 enzymes. Gene fragments were cloned into pGEM-T vector with E. coli as host cells and determined the sequence of nucleotide bases. Size of the gene fragment have been found 539 bp using the DPE.slF and DPE.eR primer pair. The gene fragment encodes 179 amino acid residues of protein fragment. The protein fragment has high homology with levanase of Bacillus subtilis BSn5, levanase of Bacillus subtilis subsp. subtilis str 168, exoinulinase of Pseudomonas mucidolents, exoinulinase of Paenibacillus polymyxa, exoinulinase of Geobacillus stearothermophilus, exoinulinase of Paenibacillus Aloe sp-11 and exoinulinase of Paenibacillus polymyxa SC2. The homology were 97, 97, 62, 62, 61, 62 and 62%, respectively. The primers can use to isolate gene fragment that encodes inulin hydrolysis enzyme from the Bacillus genus.
 
 
 
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