How to approach heterogeneous protein expression for biotechnological use: An overview

Production of recombinant proteins in Escherichia coli expression systems has shown many advantages, as well as disadvantages, especially for biotechnological and other down-stream applications. The choice of an appropriate vector depends on the gene, to be cloned for purification procedures and oth...

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Main Authors: Jamrichová Daniela, Tišáková Lenka, Jarábková Veronika, Godány Andrej
Format: Article
Language:English
Published: SciCell s.r.o. 2017-06-01
Series:Nova Biotechnologica et Chimica
Subjects:
Online Access:http://www.degruyter.com/view/j/nbec.2017.16.issue-1/nbec-2017-0001/nbec-2017-0001.xml?format=INT
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author Jamrichová Daniela
Tišáková Lenka
Jarábková Veronika
Godány Andrej
author_facet Jamrichová Daniela
Tišáková Lenka
Jarábková Veronika
Godány Andrej
author_sort Jamrichová Daniela
collection DOAJ
description Production of recombinant proteins in Escherichia coli expression systems has shown many advantages, as well as disadvantages, especially for biotechnological and other down-stream applications. The choice of an appropriate vector depends on the gene, to be cloned for purification procedures and other analyses. Selection of a suitable production strain plays an important role in the preparation of recombinant proteins. The main criteria for the selection of the host organism are the properties of the recombinant produced protein, its subsequent use and the total amount desired. The most common problems in eukaryotic gene expression and recombinant proteins purification are, for instance, post-translational modifications, formation of disulphide bonds, or inclusion bodies. Obtaining a purified protein is a key step enabling further characterization of its role in the biological system. Moreover, methods of protein purification have been developed in parallel with the discovery of proteins and the need for their studies and applications. After protein purification, and also between the individual purification steps, it is necessary to test protein stability under different conditions over time. Shortly, all the essential points have been briefly discussed, which could be encountered during production and purification of a recombinant protein of interest, especially from eukaryotic source and expressed heterogeneously in prokaryotic production system.
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spelling doaj.art-7a029ee2b78c41c49a00d82a1d9d712b2022-12-22T02:30:45ZengSciCell s.r.o.Nova Biotechnologica et Chimica1338-69052017-06-0116111110.1515/nbec-2017-0001nbec-2017-0001How to approach heterogeneous protein expression for biotechnological use: An overviewJamrichová Daniela0Tišáková Lenka1Jarábková Veronika2Godány Andrej3Department of Biology, Faculty of Natural Sciences, University of SS. Cyril and Methodius in Trnava, Nám. J. Herdu 2, Trnava, SK-917 01, Slovak RepublicDepartment of Biology, Faculty of Natural Sciences, University of SS. Cyril and Methodius in Trnava, Nám. J. Herdu 2, Trnava, SK-917 01, Slovak RepublicDepartment of Biology, Faculty of Natural Sciences, University of SS. Cyril and Methodius in Trnava, Nám. J. Herdu 2, Trnava, SK-917 01, Slovak RepublicDepartment of Biology, Faculty of Natural Sciences, University of SS. Cyril and Methodius in Trnava, Nám. J. Herdu 2, Trnava, SK-917 01, Slovak RepublicProduction of recombinant proteins in Escherichia coli expression systems has shown many advantages, as well as disadvantages, especially for biotechnological and other down-stream applications. The choice of an appropriate vector depends on the gene, to be cloned for purification procedures and other analyses. Selection of a suitable production strain plays an important role in the preparation of recombinant proteins. The main criteria for the selection of the host organism are the properties of the recombinant produced protein, its subsequent use and the total amount desired. The most common problems in eukaryotic gene expression and recombinant proteins purification are, for instance, post-translational modifications, formation of disulphide bonds, or inclusion bodies. Obtaining a purified protein is a key step enabling further characterization of its role in the biological system. Moreover, methods of protein purification have been developed in parallel with the discovery of proteins and the need for their studies and applications. After protein purification, and also between the individual purification steps, it is necessary to test protein stability under different conditions over time. Shortly, all the essential points have been briefly discussed, which could be encountered during production and purification of a recombinant protein of interest, especially from eukaryotic source and expressed heterogeneously in prokaryotic production system.http://www.degruyter.com/view/j/nbec.2017.16.issue-1/nbec-2017-0001/nbec-2017-0001.xml?format=INTEscherichia coli Gene expression Protein purification Heterologous
spellingShingle Jamrichová Daniela
Tišáková Lenka
Jarábková Veronika
Godány Andrej
How to approach heterogeneous protein expression for biotechnological use: An overview
Nova Biotechnologica et Chimica
Escherichia coli Gene expression Protein purification Heterologous
title How to approach heterogeneous protein expression for biotechnological use: An overview
title_full How to approach heterogeneous protein expression for biotechnological use: An overview
title_fullStr How to approach heterogeneous protein expression for biotechnological use: An overview
title_full_unstemmed How to approach heterogeneous protein expression for biotechnological use: An overview
title_short How to approach heterogeneous protein expression for biotechnological use: An overview
title_sort how to approach heterogeneous protein expression for biotechnological use an overview
topic Escherichia coli Gene expression Protein purification Heterologous
url http://www.degruyter.com/view/j/nbec.2017.16.issue-1/nbec-2017-0001/nbec-2017-0001.xml?format=INT
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