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  - http://dx.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  - Wendorff, Marion
A1  - Eggert, Thorsten
A1  - Pohl, Martina
A1  - Dresen, Carola
A1  - Müller, Michael
A1  - Jaeger, Karl-Erich
A1  - Sprenger, Georg A.
A1  - Schürmann, Melanie
A1  - Schürmann, Martin
A1  - Johnen, Sandra
A1  - Sprenger, Gerda
A1  - Sahm, Hermann
A1  - Inoue, Tomoyuki
A1  - Schörken, Ulrich
A1  - Breittaupt, Holger
A1  - Frölich, Bettina
A1  - Heim, Petra
A1  - Iding, Hans
A1  - Juchem, Bettina
A1  - Siegert, Petra
A1  - Kula, Maria-Regina
A1  - Weckbecker, Andrea
A1  - Hummel, Werner
A1  - Fessner, Wolf-Dieter
A1  - Elling, Lothar
A1  - Wolberg, Michael
A1  - Bode, Silke
A1  - Feldmann, Ralf
A1  - Geilenkirchen, Petra
A1  - Schubert, Thomas
A1  - Walter, Lydia
A1  - Dünnwald, Thomas
A1  - Demir, Ayhan S.
A1  - Kolter-Jung, Doris
A1  - Nitsche, Adam
A1  - Dünkelmann, Pascal
A1  - Cosp, Annabel
A1  - Lingen, Bettina
T1  - Catalytic asymmetric synthesis : section 2.2
T2  - Asymmetric synthesis with chemical and biological methods / ed. by Dieter Enders ...
Y1  - 2007
SN  - 978-3-527-31473-7
SP  - 298
EP  - 413
PB  - Wiley-VCH
CY  - Weinheim
ER  -