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      Pichia pastoris: A highly successful expression system for optimal synthesis of heterologous proteins

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          Abstract

          One of the most important branches of genetic engineering is the expression of recombinant proteins using biological expression systems. Nowadays, different expression systems are used for the production of recombinant proteins including bacteria, yeasts, molds, mammals, plants, and insects. Yeast expression systems such as Saccharomyces cerevisiae ( S. cerevisiae) and Pichia pastoris ( P. pastoris) are more popular. P. pastoris expression system is one of the most popular and standard tools for the production of recombinant protein in molecular biology. Overall, the benefits of protein production by P. pastoris system include appropriate folding (in the endoplasmic reticulum) and secretion (by Kex2 as signal peptidase) of recombinant proteins to the external environment of the cell. Moreover, in the P. pastoris expression system due to its limited production of endogenous secretory proteins, the purification of recombinant protein is easy. It is also considered a unique host for the expression of subunit vaccines which could significantly affect the growing market of medical biotechnology. Although P. pastoris expression systems are impressive and easy to use with well‐defined process protocols, some degree of process optimization is required to achieve maximum production of the target proteins. Methanol and sorbitol concentration, Mut forms, temperature and incubation time have to be adjusted to obtain optimal conditions, which might vary among different strains and externally expressed protein. Eventually, optimal conditions for the production of a recombinant protein in P. pastoris expression system differ according to the target protein.

          Abstract

          The Pichia pastoris ( P. pastoris) has also been established as a versatile cell factory for the production of thousands of biomolecules both on a laboratory and industrial scale. Optimal conditions for the production of a recombinant protein in P. pastoris expression system differ according to the target protein.

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          Most cited references141

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          Recombinant protein expression in Escherichia coli

          F Baneyx (1999)
          Escherichia coli is one of the most widely used hosts for the production of heterologous proteins and its genetics are far better characterized than those of any other microorganism. Recent progress in the fundamental understanding of transcription, translation, and protein folding in E. coli, together with serendipitous discoveries and the availability of improved genetic tools are making this bacterium more valuable than ever for the expression of complex eukaryotic proteins.
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            Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris.

            The Pichia pastoris expression system offers economy, ease of manipulation, the ability to perform complex post-translational modifications, and high expression levels. Using this system, recent advances have been made in the quality of recombinant proteins in fermenter culture and in the quality of the protein product, namely improved secretion signals and glycosylation patterns.
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              Cultivation strategies to enhance productivity of Pichia pastoris: A review.

              Pichia pastoris, a methylotrophic yeast, is an established system for the production of heterologous proteins, particularly biopharmaceuticals and industrial enzymes. To maximise and optimise the production of recombinant products, recent molecular research has focused on numerous issues including the design of expression vectors, optimisation of gene copy number, co-expression of secretory proteins such as chaperones, engineering of glycosylation and secretory pathways, etc. However, the physiological effects of different cultivation strategies are often difficult to separate from the molecular effects of the gene construct (e.g., cellular stress through over-expression or incorrect post-translational processing). Hence, overall system optimisation is difficult, even though it is urgently required in order to describe and understand the behaviour of new molecular constructs. This review focuses on particular aspects of recombinant protein production related to variations in biomass growth and their implications for strain design and screening, as well as on the concept of rational comparisons between cultivation systems for the development of specific production processes in bioreactors. The relationship between specific formation rates of secreted recombinant proteins, qp, and specific growth rates, μ, has been analysed in a conceptual attempt to compare different systems, particularly those based on AOX1/methanol and GAP/glucose, and this has now evolved into a pivotal concept for bioprocess engineering of P. pastoris.
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                Author and article information

                Contributors
                farsianih@mums.ac.ir
                Journal
                J Cell Physiol
                J. Cell. Physiol
                10.1002/(ISSN)1097-4652
                JCP
                Journal of Cellular Physiology
                John Wiley and Sons Inc. (Hoboken )
                0021-9541
                1097-4652
                14 February 2020
                : 10.1002/jcp.29583
                Affiliations
                [ 1 ] Department of Microbiology and Virology, School of Medicine Jiroft University of Medical Sciences Jiroft Iran
                [ 2 ] School of Medicine, Mashhad University of Medical Sciences Inflammation and Inflammatory Diseases Research Centre Mashhad Iran
                [ 3 ] Mashhad University of Medical Sciences Antimicrobial Resistance Research Center Mashhad Iran
                Author notes
                [*] [* ] Correspondence Hadi Farsiani, Mashhad University of Medical Sciences, Antimicrobial Resistance Research Center, Azadi‐Square, Medical Campus, Mashhad 9177948564, Iran.

                Email: farsianih@ 123456mums.ac.ir

                Author information
                http://orcid.org/0000-0001-9899-2885
                http://orcid.org/0000-0001-6814-5992
                http://orcid.org/0000-0002-4738-0245
                Article
                JCP29583
                10.1002/jcp.29583
                7228273
                32057111
                43454235-674f-4cbb-95ca-42bcd10eac74
                © 2020 Wiley Periodicals, Inc.

                This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.

                History
                : 04 June 2019
                : 09 January 2020
                Page count
                Figures: 3, Tables: 6, Pages: 15, Words: 10856
                Categories
                Mini‐review
                Mini‐reviews
                Custom metadata
                2.0
                corrected-proof
                Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.0 mode:remove_FC converted:15.04.2020

                Anatomy & Physiology
                expression system,optimization,pichia pastoris,recombinant proteins,subunit vaccines

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