Production of recombinant proteins by yeast cells

Date

2012-09-01

Author

Celik, Eda
Çalık, Pınar

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

233
views

0
downloads

Yeasts are widely used in production of recombinant proteins of medical or industrial interest. For each individual product, the most suitable expression system has to be identified and optimized, both on the genetic and fermentative level, by taking into account the properties of the product, the organism and the expression cassette. There is a wide range of important yeast expression hosts including the species Saccharomyces cerevisiae, Pichia pastoris, Hansenula polymorpha, Kluyveromyces lactis, Schizosaccharomyces pombe, Yarrowia lipolytica and Arxula adeninivorans, with various characteristics such as being thermo-tolerant or halo-tolerant, rapidly reaching high cell densities or utilizing unusual carbon sources. Several strains were also engineered to have further advantages, such as humanized glycosylation pathways or lack of proteases. Additionally, with a large variety of vectors. promoters and selection markers to choose from, combined with the accumulated knowledge on industrial-scale fermentation techniques and the current advances in the post-genomic technology, it is possible to design more cost-effective expression systems in order to meet the increasing demand for recombinant proteins and glycoproteins. In this review, the present status of the main and most promising yeast expression systems is discussed.

Subject Keywords

Biotechnology

URI

https://hdl.handle.net/11511/36587

Journal

BIOTECHNOLOGY ADVANCES

DOI

https://doi.org/10.1016/j.biotechadv.2011.09.011

Collections

Department of Chemical Engineering, Article

Suggestions

OpenMETU
Core

Recombinant therapeutic protease production by Bacillus sp. Korkmaz, Nuriye; Çalık, Pınar; Department of Chemical Engineering (2007) The first aim of this study is the development of extracellular recombinant therapeutic protease streptokinase producing Bacillus sp., and the second aim is to determine fermentation characteristics for streptokinase production. In this context, the signal (pre-) DNA sequence of B.licheniformis (DSM1969) extracellular serine alkaline protease enzyme gene (subC: Acc. No. X03341) was ligated to 5’ end of the streptokinase gene (skc: Acc. No. S46536) by SOE (Gene Splicing by Overlap Extension) method through P...
Determination of metabolic bottlenecks using reaction engineering principles in serine alkaline protease production by recombinant bacillus sp. Telli, İlkin Ece; Çalık, Pınar; Department of Chemical Engineering (2004) In this study, firstly, bioprocess characteristics for Serine Alkaline Protease (SAP) production, using recombinant Bacillus subtilis carrying pHV1431::subC, were examined. The cell concentration, substrate concentration, SAP activity and SAP synthesis rate profiles demonstrated that the system reaches to a steady state in terms of cell growth and SAP synthesis between t=15-25 h, therefore, this time interval is appropriate to employ both metabolic flux analysis and metabolic control analysis, which apply s...
Comparison of benzaldehyde lyase production capacity in recombinant Escherichia coli and recombinant Bacillus species Kaya, Hande; Çalık, Pınar; Department of Chemical Engineering (2006) In this study, the benzaldehyde lyase (BAL, EC 4.1.2.38) production in E. coli BL21 (DE3) pLySs as intracellular and in Bacillus species as extracellular were investigated, and comparison of the production capacity of the enzyme in the developed recombinant microorganisms were compared. For this purpose, firstly, PCR amplified bal gene was cloned into pRSETA vector which is under the control of strong T7 promoter and expressed in E. coli BL21 (DE3) pLysS strain. With developed recombinant E. coli BL21 (DE3)...
Affinity purification and characterization of a G-protein coupled receptor, Saccharomyces cerevisiae Ste2p Lee, Byung-Kwon; Jung, Kyung-Sik; Son, Çağdaş Devrim; Kini, Heejung; VerBerknioes, Nathan C.; Arshava, Boris; Naider, Fred; Becker, Jeffrey M. (Elsevier BV, 2007-11-01) We present an example of expression and purification of a biologically active G-protein coupled receptor (GPCR) from yeast. An expression vector was constructed to encode the Saccharomyces cerevisiae GPCR a-factor receptor (Ste2p, the STE2 gene product) containing a 9-amino acid sequence of rhodopsin that served as an epitope/affinity tag. In the construct, two glycosylation sites and two cysteine residues were removed to aid future structural and functional studies. The receptor was expressed in yeast cell...
The effects of twelve quorum-sensing gene products on the expression of bacabcde operon in bacillus subtilis Öğülür, İsmail; Özcengiz, Gülay; Department of Biotechnology (2008) In Bacillus subtilis, genetic competence, sporulation and antibiotic production are controlled by quorum-sensing global regulatory mechanism. Bacilysin, being produced and excreted by certain strains of Bacillus subtilis, is a dipeptide antibiotic composed of L-alanine and L-anticapsin. We showed that the biosynthesis of bacilysin is under the control of quorum sensing global regulatory pathway through the action of ComQ/ComX, PhrC (CSF), ComP/ComA in a Spo0K (Opp)-dependent manner. Recently, the ywfBCDEF g...

Citation Formats

E. Celik and P. Çalık, “Production of recombinant proteins by yeast cells,” BIOTECHNOLOGY ADVANCES, pp. 1108–1118, 2012, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/36587.