Article Per Year (5 Year)
p-Index From 2019 - 2024
0.61
P-Index
This Author published in this journals
All Journal Jurnal Kimia (Journal of Chemistry) Jurnal Ilmu Dasar Indonesian Journal of Pharmaceutical Science and Technology MPI (Media Pharmaceutica Indonesiana) JURNAL BIOLOGI INDONESIA Kinetik: Game Technology, Information System, Computer Network, Computing, Electronics, and Control Indonesian Journal of Chemistry ANNALES BOGORIENSES Berkala Penelitian Hayati Makara Journal of Technology
Ni Nyoman Tri Puspaningsih
Department Of Chemistry, Faculty Of Science And Technology, Airlangga University
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Civil Engineering, Building, Construction & Architecture Computer Science & IT Control & Systems Engineering Electrical & Electronics Engineering Energy Engineering Health Professions Immunology & microbiology Materials Science & Nanotechnology Mathematics Mechanical Engineering Medicine & Pharmacology

Published : 21 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 21 Documents
Search

 1   2   3 
Pencirian Produksi Amilase oleh Saccaromyces cerevisiae W303A Rekombinan Thontowi, Ahmad; Puspaningsih, Ni Nyoman Tri; Hadi, Sofjan; Purkan, Purkan; Irawan, Bambang
JURNAL BIOLOGI INDONESIA Vol 3, No 3 (2002): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (398.112 KB) | DOI: 10.14203/jbi.v3i3.3464

Abstract

ABSTRACTCharacterization of Amylase Production by Saccharomyces cerevisiae W303A Recombinants. Cloning of amylase gene from Endomycopsis fibuligera ITB.R.cc.64 into S. cerevisiae W303a can effectively increase the yeast function to digest starch directly into ethanol. Production of amylase by S. cerevisiae W303a recombinants (I and P) were done by growing in yeast peptone starch (YPS) medium. The result showed that the recombinants could be produced of amylase by gave clear zone after staining by iodium vapor. The optimum condition of production of amylase by S. cerevisiae W303a recombinants were pH 7.0, 40?C temperature incubation, and gave maximum activity after 36 hours incubation. Amylase activity of I was higher than P recombinant for these condition respectively.Key words: Characterization, amylase, S. cerevisiae W303a
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 | 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
PENCIRIAN PRODUKSI AMILASE OLEH SACCAROMYCES CEREVISIAE W303A REKOMBINAN Thontowi, Ahmad; Puspaningsih, Ni Nyoman Tri; Hadi, Sofjan; Purkan, Purkan; Ni'mahtuzahroh, Ni'mahtuzahroh; Irawan, Bambang
JURNAL BIOLOGI INDONESIA Vol 3, No 3 (2002): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jbi.v3i3.3464

Abstract

ABSTRACTCharacterization of Amylase Production by Saccharomyces cerevisiae W303A Recombinants. Cloning of amylase gene from Endomycopsis fibuligera ITB.R.cc.64 into S. cerevisiae W303a can effectively increase the yeast function to digest starch directly into ethanol. Production of amylase by S. cerevisiae W303a recombinants (I and P) were done by growing in yeast peptone starch (YPS) medium. The result showed that the recombinants could be produced of amylase by gave clear zone after staining by iodium vapor. The optimum condition of production of amylase by S. cerevisiae W303a recombinants were pH 7.0, 40?C temperature incubation, and gave maximum activity after 36 hours incubation. Amylase activity of I was higher than P recombinant for these condition respectively.Key words: Characterization, amylase, S. cerevisiae W303a
FRAKSINASI AMONIUM SULFAT PADA ENZIM ?-L-ARABINOFURANOSIDASE TERMOSTABIL I Nengah Wirajana; Ni Nyoman Tri Puspaningsih
Jurnal Kimia (Journal of Chemistry) Vol. 5, No. 2 Juli 2011
Publisher : Program Studi Kimia, FMIPA, Universitas Udayana (Program of Study in Chemistry, Faculty of Mathematics and Natural Sciences, Udayana University), Bali, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (283.197 KB)

Abstract

?-L-Arabinofuranosidases (EC 3.2.1.55) catalyze the hydrolysis ?-L-arabinofuranosidic bonds and act synergistically with other hemicellulases enzymes for the complete hydrolysis of hemicelluloses. Yeast Saccharomyces cerevisiae that considered as Generally Recognized As Safe (GRAS) was chosen for expression and secretion of thermostable ?-L-arabinofuranosidase (AbfA) from Geobacillus thermoleovorans IT-08 termofilik dengan teknologi DNA rekombinan. The extracellular enzyme from the secretion result in this recombinant yeast was precipitated with ammonium sulphate fractionation. Base on the result of measurement of the enzyme activity and the concentration of total protein showed that the specific activity of AbfA enzyme was the lowest at 40% saturation of ammonium sulfat, and the highest at 80% saturation of ammonium sulfat.
SUBKLONING GEN -L-ARABINOFURANOSIDASE (abfA) DALAM VEKTOR EKSPRESI pYES2 I Nengah Wirajana; Eddy Bagus Wasito; H.M. Soekry Erfan Kusuma; Ni Nyoman Tri Puspaningsih
Jurnal Kimia (Journal of Chemistry) Vol. 4, No. 2 Juli 2010
Publisher : Program Studi Kimia, FMIPA, Universitas Udayana (Program of Study in Chemistry, Faculty of Mathematics and Natural Sciences, Udayana University), Bali, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (512.632 KB)

Abstract

A Gene encoding -L-arabinofuranosidase (abfa) that had been cloned into recombinant E. coliDH5a/pTP510 was subcloned into Saccharomyces cerevisiae yeast system. The aim of subcloning of abfA gene intoS. cerevisiae is to express the thermostable -L-arabinofuranosidase (AbfA) enzyme in the host that is often termedas Generally Recognized As Safe (GRAS), so that this enzyme earn the broader application like in food and beverageindustries. The gene of abfA was subcloned by the amplification of Polymerase Chain Reaction (PCR) from plasmidpTP510 templat. A pair of primers, pFSacI-Af (forward) and pXhoI-Af (reverse) from designed this research wasused for the amplifcation. The PCR condition was performed as follows : beginning denaturation at 94oC for 5 min;PCR cycle 30 times that consisted of denaturation (94oC for 1 min), annealing (55oC for 30 s), andpolymerization/extension at 72oC for 2 min; and than final extension at 72oC for 7 min. The abfA gene, resulted wasinserted between GAL1 promoter and CYT1 terminator in the pYES2 expression vector. This ligation product wastransformed into E. coli TOP10 host. Restriction analysis of recombinant plasmid from this construction, thedesignated as plasmid pY-Af, showed the expected size, about 7,4 kb, which was the summation of sizes of parentalplasmid ( 5,9 kb) and fragment of DNA insert (1,5 kb).
Screening Variables in Reducing the Brown Color from the Filtrate of Heavy Metal’s Elimination Indrajati Kohar; Soediatmoko Soediman; Mario Mario; Deby Vinolia; Ni Nyoman Tri Puspaningsih; Leon Janssen
MPI (Media Pharmaceutica Indonesiana) Vol. 1 No. 2 (2016): DECEMBER
Publisher : Fakultas Farmasi, Universitas Surabaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1261.417 KB) | DOI: 10.24123/mpi.v1i2.188

Abstract

Heavy metals contamination is a major concern in the world, and also is in Indonesia. Manyattempts have been done to reduce or even eliminate it from the environment, among other ways theuse of agriculture waste, such as rice straw. Why use rice straw? Because it is available abundantly.Many studies showed that rice straw could adsorb heavy metals from polluted water, and it is cheap.The drawback of rice straw is the color of the filtrate is brown, so that it cannot be used for everydayor household purposes. An attempt using enzyme has been tried to reduce the brown color and it didreduce the brown color. Enzyme L-α-arabino-furanosidase is used in this study. However, as there aremany variables used in the experiments, before optimization can be conducted, a screening needs to becarried out first. Type of enzyme (optimum temperature of 50oC and 70oC), incubation time and amountof enzyme, number time of washing, water for washing, place of the rice plantation (high land and lowland), and size of straw, are the variables that need to be screened. The variables that gives the highestresponse in this study were enzyme-50, amount of enzyme : straw = 2 : 1 (10 ml of enzyme for each 5g of straw), 1 hour incubation time, amount of washing : 5 x 5 ml, place of plant: low land, and size ofstraw: ground. As for the type of washing liquid, both either demineralised water or Pb solution were thesame. However, the variables are still need to be reduced, and the experiment/study will be continuedto optimize the reduced variables.
Production and Characterization of Enzyme β-Endoxylanase from Bacteria of Termite-intestinal System A. A. Istri Ratnawati; Wuryanti Handayani; Ni Nyoman Tri Puspaningsih
Jurnal ILMU DASAR Vol 8 No 2 (2007)
Publisher : Fakultas Matematika dan Ilmu Pengetahuan Alam Universitas Jember

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (111.567 KB)

Abstract

A mesophile bacteria isolated from intestinal systems of local-soil termite, produced an extracellular β-endoxylanase upon growth on xylan. Optimum production of the enzyme was found in media containing oatspelt xylan at 37oC after sixth hours. The activities of its β-endoxylanase on oat-spelt xylan was investigated. It had an optimum pH and temperature, 5.0 and 40o C, respectively. However, pH stability occurred between 5.08.0. The enzyme was stable at 40o C for four hours and possessed a half life of four hours. β-endoxylanase had an apparent molecular mass of 45.000 to 66.200 Dalton as determined by SDS-PAGE. Analysis of zymogram using SDS-Xylan-PAGE indicated that enzymes could degrade oat-spelt xylan as substrates.
Cloning, Sequencing and Characterization of The Xylan Degrading Enzymes from Geobacillus thermoleovorans IT-08 Ni Nyoman Tri Puspaningsih; Antonius Suwanto; Maggy T Suhartono
Jurnal ILMU DASAR Vol 9 No 2 (2008)
Publisher : Fakultas Matematika dan Ilmu Pengetahuan Alam Universitas Jember

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (305.475 KB)

Abstract

Geobacillus thermoleovorans IT-08 is a Gram positive, thermophilic bacterium that can utilize xylan as a sole source of carbon. This strain was isolated from Gunung Pancar hot spring, Bogor, West Java, Indonesia. A plasmid genomic library in Escherichia coli DH5α was constructed and screened for xylanase activity. One positive clone, namely DH5α (pTP510) has been isolated, sequenced and showed putative exo-xylanase (exo-xyl), β-xylosidase (xyl), and α-L-arabinofuranosidase (abfa) genes (Genebank Accession No.DQ387047, DQ345777 and DQ387046 respectively). Each gene encoded 604, 511 and 502 amino acids, respectively. The BLAST search for protein database revealed that Abfa was high similar with GH51 family Abfa of Geobacillus stearothermophilus T6, but Xyl and Exo-Xyl were slight similar with GH43 family (25-34%) respectively. The deduced protein had a molecular weight of about 70 kDa (Exo-Xyl), and 60 kDa (Xyl and Abfa). These showed good accordance with the calculated molecular weight of each protein (68.64 kDa for Exo-xyl, 57.99 kDa for Xyl and 57.03 kDa for Abfa) from deduced amino acid sequence.
ISOLASI DAN KARAKTERISASI MUTAN sal4 DI RAGI Saccharomyces cereviceae Ni Nyoman Tri Puspaningsih
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 1 No 1 (1995): June 1995
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (385.012 KB) | DOI: 10.23869/164

Abstract

Recently, genetics manipulation in yeast Saccharomyces cereviceae have much been done. It because yeast can be used as a host cell alternative in the foreign protein expression, therefore information about fidelity from yeast should be studied. Preliminary study showed that SAL 4 gene has assumed to has a role in translation fidelity control and/or termination factor. To study the gene function, mutation in yeast BSC483/1a has been done by Ethylmethane sulphonate. Mutants wished are mutated at sal 4 locus and have characteristic of both allosuppressor and omnipotent suppressor. Phenotype of allosuppresor mutants were indicated by white colour consistency in YPD and Y8 medium, temperature sensitivity, paromomycin sensitivity and growth rate. Quantitatively, effectiveness as omnipotent suppressor has been done by using gene fusion between PGK and B-galaktosidase. The result showed that BSC483/1a strain could be mutated by Ethylmethane sulphonate 1% and produced eight allosuppressor mutants. Two of them (Number 8 and 10) have characteristic of temperature sensitivity, and the two others (Number 1 and 13) were mutated at sal 4 gene locus. Characterize of sal 4 mutants (1 and 13) didn't show temperature sensitive and have growth rate relatively more slowly than the wild type. Mutant (number 13) could suppress nonsense mutation (realthrough) at termination codon UAG with B-galaktosidase activity as amount 2.70 unit/ml.
KARAKTERISASI EKSTRAK KASAR FITASE TERMOFILIK DARI BAKTERI KAWAH IJEN BANYUWANGI, ISOLAT AP-17 Aline Puspita Kusumadjaja; Tutuk Budiati; Sajidan; Ni Nyoman Tri Puspaningsih
JURNAL PENELITIAN BIOLOGI BERKALA PENELITIAN HAYATI Vol 16 No 1 (2010): December 2010
Publisher : The East Java Biological Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.23869/277

Abstract

Crude thermophilic phytase was produced by isolate AP-17 that has been isolated from Ijen Crater Banyuwangi. Based on Gram test, isolate AP-17 was gram positive spore forming rod shape bacteria so that it was identified as Bacillus sp. AP-17. Crude thermophilic phytase isolated from Bacillus sp. AP-17 had the optimum temperature at 75° C with activity of 0.1413 U/ml, and its optimum pH was at pH 6 with activity of 0.0875 U/ml. The enzyme was stable when heated at 75° C for three hours and still had 90% activity when it was exposed at pH 5–8, optimum temperature, for one hour.
Co-Authors A. A. Istri Ratnawati A.A. Ketut Agung Cahyawan W AFAF BAKTIR Ahmad Thontowi Akhmaloka Akhmaloka Akhmaloka Ali Rohman Aline Puspita Kusumadjaja Aline Puspita Kusumadjaja Ami Soewandi J.S. Ami Soewandi J.S. Antonius Suwanto dan Meity S. Sinaga . Budi Tjahjono Andi Khaeruni R Asnia Zainuddin Bambang Irawan Deby Vinolia Dinda Khoirul Ummah Eddy Bagus Wasito Evi Umayah Ulfa Ganden Supriyanto H.M. Soekry Erfan Kusuma Hadi, Sofjan Hadi, Sofjan Hanim Istatik Badi'ah Hery Suwito I Nengah Wirajana Indrajati Kohar Kazuo Sakka Kimura, Tetsuya Kusuma, Soekry Erfan Leon Janssen Maemonah, Maemonah Maggy T Suhartono Mario Mario Mohammad Hamim Zajuli Al Faroby Mohammad Isa Irawan Ni'mahtuzahroh, Ni'mahtuzahroh One Asmarani One Asmarani, One Purkan Purkan, Purkan Sajidan Sajidan Sajidan Sakka, Kazuo Soediatmoko Soediman Soekry Erfan Kusuma Sofijan Hadi Sofyan Hadi Sri Sumarsih Tetsuya Kimura Tutuk Budiati Tutuk Budiati Wardojo, Bambang Prajogo Eko Wuryanti Handayani Y. Sri Wulan Manuhara Y. Sriwulan M.