Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity

Escherichia coli , one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving th...

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Published in:Microbial cell factories Vol. 21; no. 1; pp. 1 - 18
Main Authors: Zhang, Zi-Xu, Nong, Fang-Tong, Wang, Yu-Zhou, Yan, Chun-Xiao, Gu, Yang, Song, Ping, Sun, Xiao-Man
Format: Journal Article
Language:English
Published: London BioMed Central 15.09.2022
BioMed Central Ltd
Springer Nature B.V
BMC
Subjects:
Applied Microbiology
Bacterial proteins
Binding sites
Biotechnology
Chemistry
Chemistry and Materials Science
E coli
Engineering research
Enzymes
Enzymology
Escherichia coli
Fermentation
Food industry
Genetic Engineering
Genomes
Gram-positive bacteria
Host burden
Inclusion bodies
Methods
Microbial Genetics and Genomics
Microbiological synthesis
Microbiology
Mutation
Optimization
Physiological aspects
Post-translational modification
Production capacity
Production processes
Protein biosynthesis
Protein engineering
Protein expression
Protein folding
Proteins
Recombinant protein
Recombinant proteins
Review
RNA polymerase
Toxicity
China
Post-translational modification
Recombinant protein
Inclusion bodies
Host burden
ISSN:1475-2859, 1475-2859
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Abstract Escherichia coli , one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving this problem is to alleviate the host burden associated with protein overproduction and to enhance the ability to accurately fold and modify RPs at high expression levels. Here, we summarize the recently developed optimization strategies for the high-level production of RPs from the two aspects of host burden and protein activity. The aim is to maximize the ability of researchers to quickly select an appropriate optimization strategy for improving the production of RPs.
AbstractList Abstract Escherichia coli, one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving this problem is to alleviate the host burden associated with protein overproduction and to enhance the ability to accurately fold and modify RPs at high expression levels. Here, we summarize the recently developed optimization strategies for the high-level production of RPs from the two aspects of host burden and protein activity. The aim is to maximize the ability of researchers to quickly select an appropriate optimization strategy for improving the production of RPs.
Escherichia coli, one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving this problem is to alleviate the host burden associated with protein overproduction and to enhance the ability to accurately fold and modify RPs at high expression levels. Here, we summarize the recently developed optimization strategies for the high-level production of RPs from the two aspects of host burden and protein activity. The aim is to maximize the ability of researchers to quickly select an appropriate optimization strategy for improving the production of RPs. Keywords: Escherichia coli, Recombinant protein, Host burden, Post-translational modification, Inclusion bodies
Escherichia coli , one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving this problem is to alleviate the host burden associated with protein overproduction and to enhance the ability to accurately fold and modify RPs at high expression levels. Here, we summarize the recently developed optimization strategies for the high-level production of RPs from the two aspects of host burden and protein activity. The aim is to maximize the ability of researchers to quickly select an appropriate optimization strategy for improving the production of RPs.
Escherichia coli, one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving this problem is to alleviate the host burden associated with protein overproduction and to enhance the ability to accurately fold and modify RPs at high expression levels. Here, we summarize the recently developed optimization strategies for the high-level production of RPs from the two aspects of host burden and protein activity. The aim is to maximize the ability of researchers to quickly select an appropriate optimization strategy for improving the production of RPs.Escherichia coli, one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving this problem is to alleviate the host burden associated with protein overproduction and to enhance the ability to accurately fold and modify RPs at high expression levels. Here, we summarize the recently developed optimization strategies for the high-level production of RPs from the two aspects of host burden and protein activity. The aim is to maximize the ability of researchers to quickly select an appropriate optimization strategy for improving the production of RPs.
Escherichia coli, one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving this problem is to alleviate the host burden associated with protein overproduction and to enhance the ability to accurately fold and modify RPs at high expression levels. Here, we summarize the recently developed optimization strategies for the high-level production of RPs from the two aspects of host burden and protein activity. The aim is to maximize the ability of researchers to quickly select an appropriate optimization strategy for improving the production of RPs.
ArticleNumber 191
Audience Academic
Author Yan, Chun-Xiao
Song, Ping
Sun, Xiao-Man
Zhang, Zi-Xu
Wang, Yu-Zhou
Nong, Fang-Tong
Gu, Yang
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  organization: School of Food Science and Pharmaceutical Engineering, Nanjing Normal University
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  surname: Sun
  fullname: Sun, Xiao-Man
  email: xiaomansun@njnu.edu.cn
  organization: School of Food Science and Pharmaceutical Engineering, Nanjing Normal University
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Issue 1
Keywords Post-translational modification
Recombinant protein
Inclusion bodies
Host burden
Language English
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Snippet Escherichia coli , one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries....
Escherichia coli, one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries....
Abstract Escherichia coli, one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other...
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SubjectTerms Applied Microbiology
Bacterial proteins
Binding sites
Biotechnology
Chemistry
Chemistry and Materials Science
E coli
Engineering research
Enzymes
Enzymology
Escherichia coli
Fermentation
Food industry
Genetic Engineering
Genomes
Gram-positive bacteria
Host burden
Inclusion bodies
Methods
Microbial Genetics and Genomics
Microbiological synthesis
Microbiology
Mutation
Optimization
Physiological aspects
Post-translational modification
Production capacity
Production processes
Protein biosynthesis
Protein engineering
Protein expression
Protein folding
Proteins
Recombinant protein
Recombinant proteins
Review
RNA polymerase
Toxicity
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Title Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity
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