Details
| Original language | English |
|---|---|
| Pages (from-to) | 1382-1395 |
| Number of pages | 14 |
| Journal | Biotechnology advances |
| Volume | 32 |
| Issue number | 8 |
| Publication status | Published - 2 Sept 2014 |
Abstract
Many enzymes from basidiomycota have been identified and more recently characterized on the molecular level. This report summarizes the potential biotechnological applications of these enzymes and evaluates recent advances in their heterologous expression in Escherichia coli. Being one of the most widely used hosts for the production of recombinant proteins, there are, however, recurrent problems of recovering substantial yields of correctly folded and active enzymes. Various strategies for the efficient production of recombinant proteins from basidiomycetous fungi are reviewed including the current knowledge on vectors and expression strains, as well as methods for enhancing the solubility of target expression products and their purification. Research efforts towards the refolding of recombinant oxidoreductases and hydrolases are presented to illustrate successful production strategies.
Keywords
- Basidiomycota, Escherichia coli, Heterologous expression, Hydrolase, Oxidoreductase, Refolding
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: Biotechnology advances, Vol. 32, No. 8, 02.09.2014, p. 1382-1395.
Research output: Contribution to journal › Article › Research
}
TY - JOUR
T1 - Escherichia coli as a production host for novel enzymes from basidiomycota
AU - Zelena, Katerina
AU - Eisele, Nadine
AU - Berger, Ralf G.
N1 - Funding information: Support of the work by the BMBF cluster Biokatalyse2021 ( FKZ0315172B ) is gratefully acknowledged.
PY - 2014/9/2
Y1 - 2014/9/2
N2 - Many enzymes from basidiomycota have been identified and more recently characterized on the molecular level. This report summarizes the potential biotechnological applications of these enzymes and evaluates recent advances in their heterologous expression in Escherichia coli. Being one of the most widely used hosts for the production of recombinant proteins, there are, however, recurrent problems of recovering substantial yields of correctly folded and active enzymes. Various strategies for the efficient production of recombinant proteins from basidiomycetous fungi are reviewed including the current knowledge on vectors and expression strains, as well as methods for enhancing the solubility of target expression products and their purification. Research efforts towards the refolding of recombinant oxidoreductases and hydrolases are presented to illustrate successful production strategies.
AB - Many enzymes from basidiomycota have been identified and more recently characterized on the molecular level. This report summarizes the potential biotechnological applications of these enzymes and evaluates recent advances in their heterologous expression in Escherichia coli. Being one of the most widely used hosts for the production of recombinant proteins, there are, however, recurrent problems of recovering substantial yields of correctly folded and active enzymes. Various strategies for the efficient production of recombinant proteins from basidiomycetous fungi are reviewed including the current knowledge on vectors and expression strains, as well as methods for enhancing the solubility of target expression products and their purification. Research efforts towards the refolding of recombinant oxidoreductases and hydrolases are presented to illustrate successful production strategies.
KW - Basidiomycota
KW - Escherichia coli
KW - Heterologous expression
KW - Hydrolase
KW - Oxidoreductase
KW - Refolding
UR - http://www.scopus.com/inward/record.url?scp=84912126469&partnerID=8YFLogxK
U2 - 10.1016/j.biotechadv.2014.08.006
DO - 10.1016/j.biotechadv.2014.08.006
M3 - Article
C2 - 25193252
AN - SCOPUS:84912126469
VL - 32
SP - 1382
EP - 1395
JO - Biotechnology advances
JF - Biotechnology advances
SN - 0734-9750
IS - 8
ER -