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@ARTICLE{Hemmerich:824717,
author = {Hemmerich, Johannes and Rohe, Peter and Kleine, Britta and
Jurischka, Sarah-Kristin and Wiechert, Wolfgang and Freudl,
Roland and Oldiges, Marco},
title = {{U}se of a {S}ec signal peptide library from {B}acillus
subtilis for the optimization of cutinase secretion in
{C}orynebacterium glutamicum},
journal = {Microbial cell factories},
volume = {15},
number = {1},
issn = {1475-2859},
address = {London},
publisher = {Biomed Central},
reportid = {FZJ-2016-07275},
pages = {208},
year = {2016},
abstract = {Technical bulk enzymes represent a huge market, and the
extracellular production of such enzymes is favorable due to
lowered cost for product recovery. Protein secretion can be
achieved via general secretion (Sec) pathway. Specific
sequences, signal peptides (SPs), are necessary to direct
the target protein into the translocation machinery. For
example, >150 Sec-specific SPs have been identified for
Bacillus subtilis alone. As the best SP for a target protein
of choice cannot be predicted a priori, screening of
homologous SPs has been shown to be a powerful tool for
different expression organisms. While SP libraries between
closely related species were successfully applied to
optimize recombinant protein secretion, this was not
investigated for distantly related species. Therefore, in
this study a Sec SP library from low-GC firmicutes B.
subtilis is investigated to optimize protein secretion in
high-GC actinobacterium Corynebacterium glutamicum using
cutinase from Fusarium solani pisi as model protein. [...]},
cin = {IBG-1},
ddc = {610},
cid = {I:(DE-Juel1)IBG-1-20101118},
pnm = {581 - Biotechnology (POF3-581)},
pid = {G:(DE-HGF)POF3-581},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000390285500002},
doi = {10.1186/s12934-016-0604-6},
url = {https://juser.fz-juelich.de/record/824717},
}