Details
| Original language | English |
|---|---|
| Pages (from-to) | 143-161 |
| Number of pages | 19 |
| Journal | Advances in Biochemical Engineering/Biotechnology |
| Volume | 89 |
| Publication status | Published - 2004 |
| Externally published | Yes |
Abstract
Escherichia coli is a versatile organism for the production of recombinant proteins. Often, however, the recombinant protein does not reach its native, biologically active conformation within the bacterial cell but deposits as inclusion bodies. The heat-shock chaperones, a group of polypeptides omnipresent in all kingdoms of life, form a network to assist proper folding of cellular proteins, prevent their deposition and can even dissolve deposits of misfolded proteins formed during environmental stress conditions such as excessive heat. Coproduction of individual chaperones with the target protein can also reduce deposition of the recombinant protein into inclusion bodies. The selection of the suitable chaperone(s), however, is still a trial-and-error process. The wrong chaperone(s) will not lead to success, or may even negatively effect product stability or host viability. Recent progress in understanding the mechanisms and substrate specificities of the major chaperones and their roles in the chaperone network now gives some hints for a more rational choice of chaperone(s) for coproduction. Also, more specialized chaperone systems may become an alternative for application in the production of recombinant proteins.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Advances in Biochemical Engineering/Biotechnology, Vol. 89, 2004, p. 143-161.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - Roles of heat-shock chaperones in the production of recombinant proteins in Escherichia coli.
AU - Hoffmann, Frank
AU - Rinas, Ursula
PY - 2004
Y1 - 2004
N2 - Escherichia coli is a versatile organism for the production of recombinant proteins. Often, however, the recombinant protein does not reach its native, biologically active conformation within the bacterial cell but deposits as inclusion bodies. The heat-shock chaperones, a group of polypeptides omnipresent in all kingdoms of life, form a network to assist proper folding of cellular proteins, prevent their deposition and can even dissolve deposits of misfolded proteins formed during environmental stress conditions such as excessive heat. Coproduction of individual chaperones with the target protein can also reduce deposition of the recombinant protein into inclusion bodies. The selection of the suitable chaperone(s), however, is still a trial-and-error process. The wrong chaperone(s) will not lead to success, or may even negatively effect product stability or host viability. Recent progress in understanding the mechanisms and substrate specificities of the major chaperones and their roles in the chaperone network now gives some hints for a more rational choice of chaperone(s) for coproduction. Also, more specialized chaperone systems may become an alternative for application in the production of recombinant proteins.
AB - Escherichia coli is a versatile organism for the production of recombinant proteins. Often, however, the recombinant protein does not reach its native, biologically active conformation within the bacterial cell but deposits as inclusion bodies. The heat-shock chaperones, a group of polypeptides omnipresent in all kingdoms of life, form a network to assist proper folding of cellular proteins, prevent their deposition and can even dissolve deposits of misfolded proteins formed during environmental stress conditions such as excessive heat. Coproduction of individual chaperones with the target protein can also reduce deposition of the recombinant protein into inclusion bodies. The selection of the suitable chaperone(s), however, is still a trial-and-error process. The wrong chaperone(s) will not lead to success, or may even negatively effect product stability or host viability. Recent progress in understanding the mechanisms and substrate specificities of the major chaperones and their roles in the chaperone network now gives some hints for a more rational choice of chaperone(s) for coproduction. Also, more specialized chaperone systems may become an alternative for application in the production of recombinant proteins.
UR - http://www.scopus.com/inward/record.url?scp=3142726475&partnerID=8YFLogxK
U2 - 10.1007/b93996
DO - 10.1007/b93996
M3 - Review article
C2 - 15217158
AN - SCOPUS:3142726475
VL - 89
SP - 143
EP - 161
JO - Advances in Biochemical Engineering/Biotechnology
JF - Advances in Biochemical Engineering/Biotechnology
SN - 0724-6145
ER -