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    Production of a soluble and functional recombinant apolipoproteinD in the Pichia pastoris expression system

    , Article Protein Expression and Purification ; Volume 121 , 2016 , Pages 157-162 ; 10465928 (ISSN) Armanmehr, S ; Kalhor, H. R ; Tabarraei, A ; Sharif University of Technology
    Academic Press Inc 
    ApolipoproteinD (ApoD) is a human glycoprotein from the lipocalin family. ApoD contains a conserved central motif of an 8-stranded antiparallel β-sheet, which forms a beta-barrel that can be used for transport and storage of diverse hydrophobic ligands. Due to hydrophobic nature of ApoD, it has been difficult to generate a recombinant version of this protein. In the present work, we aimed at the production of ApoD in the robust Pichia pastoris expression system. To this end, the ApoD gene sequence was synthesized and subcloned for expression in the yeast host cells. Following integration of the ApoD gene into the yeast genomic region using homologous recombination, the ApoD recombinant... 

    Two-compartment processing as a tool to boost recombinant protein production

    , Article Engineering in Life Sciences ; Vol. 14, issue. 2 , March , 2014 , p. 118-128 Jazini, M ; Herwig, C ; Sharif University of Technology
    Pichia pastoris is used extensively as a production platform for many recombinant proteins. The dissolved oxygen (DO) is one of the most important factors influencing protein production. The influence of the DO on productivity has not been studied independent from the feed rate. In this work, various DO levels were investigated independent from the feed rate. The model system was recombinant P. pastoris under the control of methanol-induced alcohol oxidase promoter, which expressed HRP as the target protein. No significant effect was observed in terms of titer and specific productivity, which is a confirmation of the fact that the DO in a one-compartment system cannot boost productivity for... 

    Producing functional recombinant human keratinocyte growth factor in Pichia pastoris and investigating its protective role against irradiation

    , Article Enzyme and Microbial Technology ; Volume 111 , April , 2018 , Pages 12-20 ; 01410229 (ISSN) Bahadori, Z ; Kalhor, H. R ; Mowla, S. J ; Sharif University of Technology
    Elsevier Inc  2018
    Keratinocyte Growth Factor (KGF) is a paracrine-acting, epithelial mitogen that plays a prominent role in the regeneration of damaged epithelial tissues. In spite of different attempts to produce recombinant human KGF in many organisms, including bacteria, mammalian cells, plant cells and insect cells; production of recombinant form suffers from lower yields and recovery relative to other recombinant proteins of similar size and properties. Due to many advantages of Pichia pastoris expression systems for producing industrial enzymes and pharmaceutical proteins, in this study P. pastoris was chosen as a host for KGF expression. For preparing human KGF coding sequence, MCF-7 cell line was...