TY  - JOUR
A1  - Deppe, Veronika Maria
A1  - Bongaerts, Johannes
A1  - O'Connell, Timothy
A1  - Maurer, Karl-Heinz
A1  - Meinhardt, Friedhelm
T1  - Enzymatic deglycation of Amadori products in bacteria
JF  - Applied microbiology and biotechnology
Y1  - 2011
SN  - 1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)
VL  - Vol. 90
IS  - Iss. 2
SP  - 399
EP  - 406
PB  - Springer
CY  - Berlin
ER  - 
TY  - JOUR
A1  - Deppe, Veronika Maria
A1  - Klatte, Stephanie
A1  - Bongaerts, Johannes
A1  - Maurer, Karl-Heinz
A1  - O'Connell, Timothy
A1  - Meinhardt, Friedhelm
T1  - Genetic control of Amadori product degradation in Bacillus subtilis via regulation of frlBONMD expression by FrlR
JF  - Applied and environmental microbiology
Y1  - 2011
SN  - 1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)
VL  - Vol. 77
IS  - No. 9
SP  - 2839
EP  - 2846
PB  - American Society of Mechanical Engineers (ASME)
CY  - New York
ER  - 
TY  - JOUR
A1  - Scheele, Sandra
A1  - Oertel, Dan
A1  - Bongaerts, Johannes
A1  - Evers, Stefan
A1  - Hellmuth, Hendrik
A1  - Maurer, Karl-Heinz
A1  - Bott, Michael
A1  - Freudl, Roland
T1  - Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol–xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum
JF  - Microbial biotechnology
Y1  - 2013
SN  - 1751-7915
SP  - 202
EP  - 206
PB  - Wiley-Blackwell
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Wilming, Anja
A1  - Begemann, Jens
A1  - Kuhne, Stefan
A1  - Regestein, Lars
A1  - Bongaerts, Johannes
A1  - Evers, Stefan
A1  - Maurer, Karl-Heinz
A1  - Büchs, Jochen
T1  - Metabolic studies of γ-polyglutamic acid production in Bacillus licheniformis by small-scale continuous cultivations
JF  - Biochemical engineering journal
Y1  - 2013
SN  - 1873-295X (E-Journal); 1369-703X (Print)
VL  - Vol. 73
SP  - 29
EP  - 37
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Voigt, Birgit
A1  - Schroeter, Rebecca
A1  - Jürgen, Britta
A1  - Albrecht, Dirk
A1  - Evers, Stefan
A1  - Bongaerts, Johannes
A1  - Maurer, Karl-Heinz
A1  - Schweder, Thomas
A1  - Hecker, Michael
T1  - The response of Bacillus licheniformis to heat and ethanol stress and the role of the SigB regulon
JF  - Proteomics
Y1  - 2013
SN  - 1615-9861 (E-Journal); 1615-9853 (Print)
VL  - Vol. 13
IS  - Iss. 14
SP  - 2140
EP  - 2146
PB  - Wiley
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Rachinger, Michael
A1  - Bauch, Melanie
A1  - Strittmatter, Axel
A1  - Bongaerts, Johannes
A1  - Evers, Stefan
A1  - Maurer, Karl-Heinz
A1  - Daniel, Rolf
A1  - Liebl, Wolfgang
A1  - Liesegang, Heiko
A1  - Ehrenreich, Armin
T1  - Size unlimited markerless deletions by a transconjugative plasmid-system in Bacillus licheniformis
JF  - Journal of biotechnology
Y1  - 2013
SN  - 1873-4863 (E-Journal); 0168-1656 (Print)
VL  - Vol. 164
IS  - Iss. 4
SP  - 365
EP  - 369
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Küppers, Tobias
A1  - Steffen, Victoria
A1  - Hellmuth, Hendrik
A1  - O'Connell, Timothy
A1  - Bongaerts, Johannes
A1  - Maurer, Karl-Heinz
A1  - Wiechert, Wolfgang
T1  - Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer
JF  - Microbial cell factories
Y1  - 2014
U6  - http://dx.doi.org/10.1186/1475-2859-13-46
SN  - 1475-2859 (E-Journal)
VL  - 13
SP  - Article No. 46
PB  - BioMed Central
CY  - London
ER  - 
TY  - JOUR
A1  - Handtke, Stefan
A1  - Volland, Sonja
A1  - Methling, Karen
A1  - Albrecht, Dirk
A1  - Becher, Dörte
A1  - Nehls, Jenny
A1  - Bongaerts, Johannes
A1  - Maurer, Karl-Heinz
A1  - Lalk, Michael
A1  - Liesegang, Heiko
A1  - Voigt, Birgit
A1  - Daniel, Rolf
A1  - Hecker, Michael
T1  - Cell physiology of the biotechnological relevant bacterium Bacillus pumilus - An omics-based approach
JF  - Journal of Biotechnology
N2  - Members of the species Bacillus pumilus get more and more in focus of the biotechnological industry as potential new production strains. Based on exoproteome analysis, B. pumilus strain Jo2, possessing a high secretion capability, was chosen for an omics-based investigation. The proteome and metabolome of B. pumilus cells growing either in minimal or complex medium was analyzed. In total, 1542 proteins were identified in growing B. pumilus cells, among them 1182 cytosolic proteins, 297 membrane and lipoproteins and 63 secreted proteins. This accounts for about 43% of the 3616 proteins encoded in the B. pumilus Jo2 genome sequence. By using GC–MS, IP-LC/MS and H NMR methods numerous metabolites were analyzed and assigned to reconstructed metabolic pathways. In the genome sequence a functional secretion system including the components of the Sec- and Tat-secretion machinery was found. Analysis of the exoproteome revealed secretion of about 70 proteins with predicted secretion signals. In addition, selected production-relevant genome features such as restriction modification systems and NRPS clusters of B. pumilus Jo2 are discussed.
Y1  - 2014
U6  - http://dx.doi.org/10.1016/j.jbiotec.2014.08.028
SN  - 1873-4863 (E-Journal); 0168-1656 (Print)
IS  - 192(A)
SP  - 204
EP  - 214
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Voigt, Birgit
A1  - Albrecht, Dirk
A1  - Sievers, Susanne
A1  - Becher, Dörte
A1  - Bongaerts, Johannes
A1  - Evers, Stefan
A1  - Schweder, Thomas
A1  - Maurer, Karl-Heinz
A1  - Hecker, Michael
T1  - High-resolution proteome maps of Bacillus licheniformis cells growing in minimal medium
JF  - Proteomics
Y1  - 2015
U6  - http://dx.doi.org/10.1002/pmic.201400504
SN  - 1615-9861
VL  - 15
IS  - 15
SP  - 2629
EP  - 2633
PB  - Wiley
CY  - Weinheim
ER  - 
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  -