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All Journal Microbiology Indonesia Jurnal Online Mahasiswa (JOM) Bidang Keguruan dan Ilmu Pendidikan eDimensi Arsitektur Petra Intra JEE (Jurnal Edukasi Ekobis) Jurnal Riset Kimia

DESSY NATALIA

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Author-ID : 433776

Biochemistry, Genetics & Molecular Biology Chemistry Civil Engineering, Building, Construction & Architecture Education Immunology & microbiology Medicine & Pharmacology

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Title

The b’x Region of Yeast Protein Disulfide Isomerase is Not Essential for Saccharomyces cerevisiae Viability at 30 °C . PURKAN; LALU RUDYAT TELLY SAVALAS; MULIAWATI SINDUMARTA; DESSY NATALIA
Microbiology Indonesia Vol. 3 No. 1 (2009): April 2009
Publisher : Indonesian Society for microbiology

Protein disulfide isomerase (PDI) catalyzes thiol oxidation, reduction and isomerization of disulphide bond of cell surface and secreted proteins. Yeast PDI1 consists of two catalytic domains (a and a’) which are separated by two non-catalytic domains (b and b’), and a x region linked the b’ and a domains. The b’ domain is important for the non-covalent binding of partially folded protein. To understand the contribution of b’ domain and x-linker of yeast PDI1 we have deleted the b’x and investigated its functional role in vitro and in vivo. Yeast PDI1 without b’x region retained only 50% activity and became more sensitive toward Proteinase K. Interestingly, yeasts containing full length PDI1 and pdi1Db’x showed approximately the same growth rate. However, the yeast pdi1Db’x mutant growth impaired severely at 37 °C compared to that of the full length PDI1. Our results suggested that the a-b-a’-c domains of PDI seems to be sufficient to support the growth of yeast cells in normal condition, but the b’x region might be essential in assisting refolding of highly accumulated unfolded protein at high temperature (37 °C).

Cloning and Expression of Endoglucanase Gene from Thermophilic Bacteria Bacillus sp. RP1 MAELITA RAMDANI MOEIS; DESSY NATALIA; RAHMA WIDYA NINGRUM; ARI DWIJAYANTI
Microbiology Indonesia Vol. 8 No. 4 (2014): December 2014
Publisher : Indonesian Society for microbiology

An endoglucanase gene from glycoside hydrolase family 5, had been isolated from Bacillus sp. RP1 and cloned into Escherichia coli. The cloned gene comprised the promoter, coding sequence and terminator of the gene.Â This gene encoded a protein with 499 amino acid residues (Mr=55.2 kDa) with a typical Bacillus signal peptide. The recombinant endoglucanase (EG) had optimum activity at pH 5.0 and 50 Â°C. The recombinant EG was expressed in the extracellular, intracellular, and periplasmic fractions with the highest total activity (60.15%) in the intracellular fraction, measured at three hours after isopropyl-Î²-Dthiogalactopyranoside (IPTG) induction. Three hours after the addition of 1% carboxymethyl cellulose (CMC), there was a two-fold increase in intracellular EG specific activity compared to the uninduced cells. Three hours after the addition of 1 mM IPTG, 1% glucose, 1% galactose or 1% cellobiose the intracellular EG specific activity decreased compared to the uninduced cells.

Heterologous Expression of Î±-Amylase from Saccharomycopsis fibuligera R64 and its Tyr401Trp Mutant in Pichia pastoris RIEZKI AMALIA; WANGSA TIRTA ISMAYA; FERNITA PUSPASARI; KHOMAINI HASAN; TOTO SUBROTO; DESSY NATALIA; SOETIJOSO SOEMITRO
Microbiology Indonesia Vol. 10 No. 1 (2016): March 2016
Publisher : Indonesian Society for microbiology

Î±-Amylase from Saccharomycopsis fibuligera R64 is a non-adsorbing raw-starch degrading enzyme, a unique characteristic. This character is difficult to explain in the absence of its three-dimensional structure. Here we discuss the expression of a-amylase from Saccharomycopsis fibuligera in Pichia pastoris and the effect of site directed mutagenesis on its activity. A model based on the structure of its homologs suggested mutation of codon of Tyr401 into that of a Trp residue. An activity study using whole cells P. pastoris showed similar substrate degradation rates by cells carrying either the native or mutant amylase encoding gene. However, the purified enzyme of the mutant strain showed faster starch hydrolysis.

Co-Authors . PURKAN ARI DWIJAYANTI FERNITA PUSPASARI Gusnardi Gusnardi I Komang Winatha Jamsari Jamsari KHOMAINI HASAN LALU RUDYAT TELLY SAVALAS MAELITA RAMDANI MOEIS Minda Azhar MULIAWATI SINDUMARTA Ngadlan Ngadlan Paulina Paulina RAHMA WIDYA NINGRUM Riezki Amalia SOETIJOSO SOEMITRO Sofiani, Sofiani Stephanus P Honggowidjaja Sumaryati Syukur Tedi Rusman Toto Subroto Vovien - WANGSA TIRTA ISMAYA

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Journal : Microbiology Indonesia