Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 16-21 |
| Seitenumfang | 6 |
| Fachzeitschrift | Journal of Molecular Catalysis B: Enzymatic |
| Jahrgang | 57 |
| Ausgabenummer | 1-4 |
| Publikationsstatus | Veröffentlicht - 27 Juni 2008 |
Abstract
The 1641 bp cDNA encoding an extra-cellular lipase of the basidiomycete Pleurotus sapidus (Lip2) was cloned from a cDNA library. Expression of the cDNA in Escherichia coli, with and without signal sequence, led to the production of recombinant Lip2, mainly as inclusion bodies with low catalytic activity. Refolding yielded catalytically active protein. A C-terminal His tag was used for purification and immunochemical detection. The recombinant lipase hydrolysed xanthophyll esters with high efficiency, and omitting the signal sequence did not alter the catalytic properties. The P. sapidus lipase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus characterised on the molecular level and expressed in a manageable host.
ASJC Scopus Sachgebiete
- Chemische Verfahrenstechnik (insg.)
- Katalyse
- Chemische Verfahrenstechnik (insg.)
- Bioengineering
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Chemische Verfahrenstechnik (insg.)
- Prozesschemie und -technologie
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in: Journal of Molecular Catalysis B: Enzymatic, Jahrgang 57, Nr. 1-4, 27.06.2008, S. 16-21.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Heterologous expression of an extra-cellular lipase from the basidiomycete Pleurotus sapidus
AU - Krügener, Sven
AU - Zelena, Kateryna
AU - Zorn, Holger
AU - Nimtz, Manfred
AU - Berger, Ralf G.
N1 - Funding information: Support of the work by the Deutsche Bundesstiftung Umwelt (AZ 13164) is gratefully acknowledged.
PY - 2008/6/27
Y1 - 2008/6/27
N2 - The 1641 bp cDNA encoding an extra-cellular lipase of the basidiomycete Pleurotus sapidus (Lip2) was cloned from a cDNA library. Expression of the cDNA in Escherichia coli, with and without signal sequence, led to the production of recombinant Lip2, mainly as inclusion bodies with low catalytic activity. Refolding yielded catalytically active protein. A C-terminal His tag was used for purification and immunochemical detection. The recombinant lipase hydrolysed xanthophyll esters with high efficiency, and omitting the signal sequence did not alter the catalytic properties. The P. sapidus lipase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus characterised on the molecular level and expressed in a manageable host.
AB - The 1641 bp cDNA encoding an extra-cellular lipase of the basidiomycete Pleurotus sapidus (Lip2) was cloned from a cDNA library. Expression of the cDNA in Escherichia coli, with and without signal sequence, led to the production of recombinant Lip2, mainly as inclusion bodies with low catalytic activity. Refolding yielded catalytically active protein. A C-terminal His tag was used for purification and immunochemical detection. The recombinant lipase hydrolysed xanthophyll esters with high efficiency, and omitting the signal sequence did not alter the catalytic properties. The P. sapidus lipase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus characterised on the molecular level and expressed in a manageable host.
KW - Basidiomycete
KW - Carboxylesterase
KW - Carotenoid ester
KW - Fungi
UR - http://www.scopus.com/inward/record.url?scp=68949090265&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2008.06.014
DO - 10.1016/j.molcatb.2008.06.014
M3 - Article
AN - SCOPUS:68949090265
VL - 57
SP - 16
EP - 21
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
SN - 1381-1177
IS - 1-4
ER -