TY  - JOUR
A1  - Degering, Christian
A1  - Eggert, Thorsten
A1  - Puls, Michael
A1  - Bongaerts, Johannes
A1  - Evers, Stefan
A1  - Maurer, Karl-Heinz
A1  - Jaeger, Karl-Erich
T1  - Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides
JF  - Applied and environmental microbiology
N2  - Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN′ from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains.
Y1  - 2010
U6  - https://doi.org/10.1128/AEM.01146-10
SN  - 1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)
VL  - 76
IS  - 19
SP  - 6370
EP  - 6378
PB  - American Society for Microbiology
CY  - Washington, DC
ER  - 
TY  - CHAP
A1  - Muffler, Kai
A1  - Tippkötter, Nils
A1  - Ulber, Roland
ED  - Timmis, Kenneth N.
T1  - Chemical feedstocks and fine chemicals from other substrates
T2  - Handbook of hydrocarbon and lipid microbiology. Volume 4:  Consequences of microbial interactions with hydrocarbons, oils and lipids. - (Springer reference)
Y1  - 2010
SN  - 978-3-540-77588-1
U6  - https://doi.org/10.1007%2F978-3-540-77587-4_214
SP  - 2891
EP  - 2902
PB  - Springer
CY  - Berlin [u.a.]
ER  - 
TY  - CHAP
A1  - Poth, Sebastian
A1  - Monzon, Magaly
A1  - Tippkötter, Nils
A1  - Ulber, Roland
T1  - Lignocellulosic biorefinery : process integration of hydrolysis and fermentation
T2  - Proceedings / 11th European Workshop on Lignocellulosics and Pulp : August 16 - 19, 2010, Hamburg, Germany
Y1  - 2010
SP  - 65
EP  - 68
PB  - vTi
CY  - Hamburg
ER  - 
TY  - JOUR
A1  - Srivastava, Alok
A1  - Singh, Virendra
A1  - Aggarwal, Pranav
A1  - Schneeweiss, F.
A1  - Scherer, Ulrich W.
A1  - Friedrich, W.
T1  - Optical studies of insulating polymers for radiation dose monitoring
JF  - Indian Journal of Pure & Applied Physics
Y1  - 2010
SN  - 0019-5596
N1  - Special Issue: SI
VL  - 48
IS  - 11
SP  - 782
EP  - 786
ER  -