Recombinant protein expression in microbial systems
With the advent of recombinant DNA technology, expressing heterologous proteins in microorganisms rapidly became the method of choice for their production at laboratory and industrial scale. Bacteria, yeasts and other hosts can be grown to high biomass levels efficiently and inexpensively. Obtaining...
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Frontiers Media SA
2021
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| Accesso online: | 17845 |
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| author | German L. Rosano Eduardo A. Ceccarelli |
| author_browse | Eduardo A. Ceccarelli German L. Rosano |
| author_facet | German L. Rosano Eduardo A. Ceccarelli |
| author_sort | German L. Rosano |
| collection | Directory of Open Access Books |
| description | With the advent of recombinant DNA technology, expressing heterologous proteins in microorganisms rapidly became the method of choice for their production at laboratory and industrial scale. Bacteria, yeasts and other hosts can be grown to high biomass levels efficiently and inexpensively. Obtaining high yields of recombinant proteins from this material was only feasible thanks to constant research on microbial genetics and physiology that led to novel strains, plasmids and cultivation strategies. Despite the spectacular expansion of the field, there is still much room for progress. Improving the levels of expression and the solubility of a recombinant protein can be quite challenging. Accumulation of the product in the cell can lead to stress responses which affect cell growth. Buildup of insoluble and biologically inactive aggregates (inclusion bodies) lowers the yield of production. This is particularly true for obtaining membrane proteins or high-molecular weight and multi-domain proteins. Also, obtaining eukaryotic proteins in a prokaryotic background (for example, plant or animal proteins in bacteria) results in a product that lack post-translational modifications, often required for functionality. Changing to a eukaryotic host (yeasts or filamentous fungi) may not be a proper solution since the pattern of sugar modifications is different than in higher eukaryotes. Still, many advances in the last couple of decades have provided to researchers a wide variety of strategies to maximize the production of their recombinant protein of choice. Everything starts with the careful selection of the host. Be it bacteria or yeast, a broad list of strains is available for overcoming codon use bias, incorrect disulfide bond formation, protein toxicity and lack of post-translational modifications. Also, a huge catalog of plasmids allows choosing for different fusion partners for improving solubility, protein secretion, chaperone co-expression, antibiotic resistance and promoter strength. Next, controlling culture conditions like temperature, inducer and media composition can bolster recombinant protein production. With this Research Topic, we aim to provide an encyclopedic account of the existing approaches to the expression of recombinant proteins in microorganisms, highlight recent discoveries and analyze the future prospects of this exciting and ever-growing field. |
| format | Online |
| id | doab-20.500.12854ir-57860 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2021 |
| publishDateRange | 2021 |
| publishDateSort | 2021 |
| publisher | Frontiers Media SA |
| publisherStr | Frontiers Media SA |
| record_format | ojs |
| spelling | doab-20.500.12854ir-578602023-12-20T12:11:11Z Recombinant protein expression in microbial systems German L. Rosano Eduardo A. Ceccarelli GE1-350 TP248.13-248.65 TA1-2040 QR1-502 Q1-390 Inclusion Bodies Escherichia coli Filamentous fungi Microalgae Recombinant Proteins Microorganism fusion tags yeast bic Book Industry Communication::K Economics, finance, business & management::KC Economics::KCN Environmental economics With the advent of recombinant DNA technology, expressing heterologous proteins in microorganisms rapidly became the method of choice for their production at laboratory and industrial scale. Bacteria, yeasts and other hosts can be grown to high biomass levels efficiently and inexpensively. Obtaining high yields of recombinant proteins from this material was only feasible thanks to constant research on microbial genetics and physiology that led to novel strains, plasmids and cultivation strategies. Despite the spectacular expansion of the field, there is still much room for progress. Improving the levels of expression and the solubility of a recombinant protein can be quite challenging. Accumulation of the product in the cell can lead to stress responses which affect cell growth. Buildup of insoluble and biologically inactive aggregates (inclusion bodies) lowers the yield of production. This is particularly true for obtaining membrane proteins or high-molecular weight and multi-domain proteins. Also, obtaining eukaryotic proteins in a prokaryotic background (for example, plant or animal proteins in bacteria) results in a product that lack post-translational modifications, often required for functionality. Changing to a eukaryotic host (yeasts or filamentous fungi) may not be a proper solution since the pattern of sugar modifications is different than in higher eukaryotes. Still, many advances in the last couple of decades have provided to researchers a wide variety of strategies to maximize the production of their recombinant protein of choice. Everything starts with the careful selection of the host. Be it bacteria or yeast, a broad list of strains is available for overcoming codon use bias, incorrect disulfide bond formation, protein toxicity and lack of post-translational modifications. Also, a huge catalog of plasmids allows choosing for different fusion partners for improving solubility, protein secretion, chaperone co-expression, antibiotic resistance and promoter strength. Next, controlling culture conditions like temperature, inducer and media composition can bolster recombinant protein production. With this Research Topic, we aim to provide an encyclopedic account of the existing approaches to the expression of recombinant proteins in microorganisms, highlight recent discoveries and analyze the future prospects of this exciting and ever-growing field. 2021-02-12T01:15:34Z 2021-02-12T01:15:34Z 2015-12-10 11:59:07 2014 book 17845 16648714 9782889192946 https://directory.doabooks.org/handle/20.500.12854/57860 eng Frontiers Research Topics image/jpeg Attribution 4.0 International http://www.frontiersin.org/books/Recombinant_protein_expression_in_microbial_systems/321#nogo http://journal.frontiersin.org/researchtopic/1381/recombinant-protein-expression-in-microbial-systems Frontiers Media SA 10.3389/978-2-88919-294-6 10.3389/978-2-88919-294-6 bf5ce210-e72e-4860-ba9b-c305640ff3ae 9782889192946 102 open access |
| spellingShingle | GE1-350 TP248.13-248.65 TA1-2040 QR1-502 Q1-390 Inclusion Bodies Escherichia coli Filamentous fungi Microalgae Recombinant Proteins Microorganism fusion tags yeast bic Book Industry Communication::K Economics, finance, business & management::KC Economics::KCN Environmental economics German L. Rosano Eduardo A. Ceccarelli Recombinant protein expression in microbial systems |
| title | Recombinant protein expression in microbial systems |
| title_full | Recombinant protein expression in microbial systems |
| title_fullStr | Recombinant protein expression in microbial systems |
| title_full_unstemmed | Recombinant protein expression in microbial systems |
| title_short | Recombinant protein expression in microbial systems |
| title_sort | recombinant protein expression in microbial systems |
| topic | GE1-350 TP248.13-248.65 TA1-2040 QR1-502 Q1-390 Inclusion Bodies Escherichia coli Filamentous fungi Microalgae Recombinant Proteins Microorganism fusion tags yeast bic Book Industry Communication::K Economics, finance, business & management::KC Economics::KCN Environmental economics |
| topic_facet | GE1-350 TP248.13-248.65 TA1-2040 QR1-502 Q1-390 Inclusion Bodies Escherichia coli Filamentous fungi Microalgae Recombinant Proteins Microorganism fusion tags yeast bic Book Industry Communication::K Economics, finance, business & management::KC Economics::KCN Environmental economics |
| url | 17845 |
| work_keys_str_mv | AT germanlrosano recombinantproteinexpressioninmicrobialsystems AT eduardoaceccarelli recombinantproteinexpressioninmicrobialsystems |