Recombinant protein expression in microbial systems (Record no. 74095)

MARC details
000 -LEADER
fixed length control field 03720naaaa2200349uu 4500
001 - CONTROL NUMBER
control field https://directory.doabooks.org/handle/20.500.12854/57860
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20220220074552.0
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 978-2-88919-294-6
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 9782889192946
024 7# - OTHER STANDARD IDENTIFIER
Standard number or code 10.3389/978-2-88919-294-6
Terms of availability doi
041 0# - LANGUAGE CODE
Language code of text/sound track or separate title English
042 ## - AUTHENTICATION CODE
Authentication code dc
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name German L. Rosano
Relationship auth
245 10 - TITLE STATEMENT
Title Recombinant protein expression in microbial systems
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Name of publisher, distributor, etc. Frontiers Media SA
Date of publication, distribution, etc. 2014
300 ## - PHYSICAL DESCRIPTION
Extent 1 electronic resource (102 p.)
506 0# - RESTRICTIONS ON ACCESS NOTE
Terms governing access Open Access
Source of term star
Standardized terminology for access restriction Unrestricted online access
520 ## - SUMMARY, ETC.
Summary, etc. 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.
540 ## - TERMS GOVERNING USE AND REPRODUCTION NOTE
Terms governing use and reproduction Creative Commons
Use and reproduction rights https://creativecommons.org/licenses/by/4.0/
Source of term cc
-- https://creativecommons.org/licenses/by/4.0/
546 ## - LANGUAGE NOTE
Language note English
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term Inclusion Bodies
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Uncontrolled term Escherichia coli
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Uncontrolled term Filamentous fungi
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Uncontrolled term Microalgae
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Uncontrolled term Recombinant Proteins
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Uncontrolled term Microorganism
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Uncontrolled term fusion tags
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term yeast
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Eduardo A. Ceccarelli
Relationship auth
856 40 - ELECTRONIC LOCATION AND ACCESS
Host name www.oapen.org
Uniform Resource Identifier <a href="http://journal.frontiersin.org/researchtopic/1381/recombinant-protein-expression-in-microbial-systems">http://journal.frontiersin.org/researchtopic/1381/recombinant-protein-expression-in-microbial-systems</a>
Access status 0
Public note DOAB: download the publication
856 40 - ELECTRONIC LOCATION AND ACCESS
Host name www.oapen.org
Uniform Resource Identifier <a href="https://directory.doabooks.org/handle/20.500.12854/57860">https://directory.doabooks.org/handle/20.500.12854/57860</a>
Access status 0
Public note DOAB: description of the publication

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