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dc.contributor.author
Ihssen, Julian
dc.contributor.author
Reiss, Renate
dc.contributor.author
Luchsinger, Ronny
dc.contributor.author
Thoeny-Meyer, Linda
dc.contributor.author
Richter, Michael
dc.date.accessioned
2018-10-11T15:25:35Z
dc.date.available
2017-06-11T18:08:24Z
dc.date.available
2018-10-11T15:25:35Z
dc.date.issued
2015-06-12
dc.identifier.issn
2045-2322
dc.identifier.other
10.1038/srep10465
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/102166
dc.identifier.doi
10.3929/ethz-b-000102166
dc.description.abstract
Laccases are multi-copper oxidases that oxidize a broad range of substrates at the expense of molecular oxygen, without any need for co-factor regeneration. These enzymes bear high potential for the sustainable synthesis of fine chemicals and the modification of (bio)polymers. Here we describe cloning and expression of five novel bacterial laccase-like multi copper oxidases (LMCOs) of diverse origin which were identified by homology searches in online databases. Activity yields under different expression conditions and temperature stabilities were compared to three previously described enzymes from Bacillus subtilis, Bacillus pumilus and Bacillus clausii. In almost all cases, a switch to oxygen-limited growth conditions after induction increased volumetric activity considerably. For proteins with predicted signal peptides for secretion, recombinant expression with and without signal sequence was investigated. Bacillus CotA-type LMCOs outperformed enzymes from Streptomyces and Gram-negative bacteria with respect to activity yields in Escherichia coli and application relevant biochemical properties. The novel Bacillus coagulans LMCO combined high activity yields in E. coli with unprecedented activity at strong alkaline pH and high storage stability, making it a promising candidate for further development.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Nature
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
Oxidoreductases
en_US
dc.subject
Industrial microbiology
en_US
dc.title
Biochemical properties and yields of diverse bacterial laccase-like multicopper oxidases expressed in Escherichia coli
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
Scientific Reports
ethz.journal.volume
5
en_US
ethz.journal.abbreviated
Sci Rep
ethz.pages.start
10465
en_US
ethz.size
13 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.nebis
006751867
ethz.publication.place
London
ethz.publication.status
published
en_US
ethz.date.deposited
2017-06-11T18:08:34Z
ethz.source
ECIT
ethz.identifier.importid
imp5936534a0902441435
ethz.ecitpid
pub:160293
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-13T14:49:36Z
ethz.rosetta.lastUpdated
2024-02-02T06:19:20Z
ethz.rosetta.versionExported
true
ethz.COinS
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