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All Journal ANNALES BOGORIENSES Makara Journal of Technology
Yana Rubiana, Yana
Research Center for Biotechnology, Indonesian Institute of Science, Cibinong, Bogor 16911, Indonesia
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Civil Engineering, Building, Construction & Architecture Electrical & Electronics Engineering Engineering Immunology & microbiology Materials Science & Nanotechnology Mechanical Engineering Medicine & Pharmacology

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In-Silico Cloning and Analysis of Divalent Subunit OMP31-SODc Proteins As A Prophylaxis Vaccine Against Brucella melitensis Infection Wijaya, Sri Kartika; Kusumawati, Arizah; Wardiana, Andri; Rubiana, Yana; Husnaa, Ulfatul; Santoso, Adi
ANNALES BOGORIENSES Vol 19, No 1 (2015): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (965.993 KB) | DOI: 10.14203/ab.v19i1.94

Abstract

The urgency to develop a new protein based subunit vaccine candidate against Brucella was provoked by its frequent infection to human and lives stock. Since Brucella melitensis is found as the most species isolated from human, thus the outer membrane of the Brucella melitensis become prominent subcellular location for searching promising antigen to be developed as vaccine target due to its interaction with cell host. Among other proteins suggested by Vaxign program, the OMP31 is found as a promising candidate. Moreover, analysis on other subcellular location leads our interest to SODc protein, which is expected to support the OMP31 in triggering immune response. The OMP31-SODc divalent vaccine candidate was analysed in-silico to predict its stable three-dimensional structure, cloning process and expectation on the ease during expression, purification and the protein vaccine delivery to develop expected immune response.
Effect of Methanol Induction and Incubation Time on Expression of Human Erythropoietin in Methylotropic Yeast Pichia Pastoris Santoso, Adi; Herawati, Neng; Rubiana, Yana
Makara Journal of Technology Vol. 16, No. 1
Publisher : UI Scholars Hub

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Abstract

Erythropoietin (EPO) is a glycoprotein hormone consists of 165 amino acids and has molecular mass of 30,400 Daltons. The large quantities of these hormone required to satisfy clinical demand are currently met by recombinant expression in mammalian cell, namely chinese hamster ovary (CHO). Pichia pastoris has become popular yeast based protein production systems to substitute mammalian expression systems. P. pastoris is capable to use methanol as sole carbon and energy source. In this study, recombinant human EPO (rhEPO) protein obtained by expressing the hEPO gene in methylotropic yeast P. pastoris, strain X33. The present work was carried out to study the optimal methanol concentration for induction and the incubation time to obtain rhEPO protein. To perform this study, the transformed P. pastoris was induced with various concentrations of methanol (0%, 0.5%, 1%, 2.5%, 5%, 10%, and 20%) and incubation times (0 hours, 24 hours, 48 hours, 72 hours, 96 hours, 120 hours, and 144 hours). The results demonstrate that the highest protein expression level occurred at concentration of 2.5% methanol induction, while the optimal incubation time was at 48 hrs.
Co-Authors A.A. Ketut Agung Cahyawan W Adi Santoso Andri Wardiana, Andri Husnaa, Ulfatul Kusumawati, Arizah Neng Herawati, Neng Wijaya, Sri Kartika