TY  - PAT
A1  - Bessler, Cornelius
A1  - Maurer, Karl-Heinz
A1  - Merkel, Marion
A1  - Siegert, Petra
A1  - Wieland, Susanne
T1  - Subtilisin from Bacillus Pumilus and detergent and cleaning agents containing said novel subtilisin [US Patentanmeldung / Internationale Patentanmeldung]
Y1  - 2009
SP  - 1
EP  - 39
PB  - USPTO; WIPO
CY  - Washington; Genf
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  - 
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  - Handtke, Stefan
A1  - Schroeter, Rebecca
A1  - Jürgen, Britta
A1  - Methling, Karen
A1  - Schlüter, Rabea
A1  - Albrecht, Dirk
A1  - Hijum, Sacha A. F. T. van
A1  - Bongaerts, Johannes
A1  - Maurer, Karl-Heinz
A1  - Lalk, Michael
A1  - Schweder, Thomas
A1  - Hecker, Michael
A1  - Voigt, Birgit
T1  - Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress
JF  - PLOS one
N2  - Bacillus pumilus is characterized by a higher oxidative stress resistance than other comparable industrially relevant Bacilli such as B. subtilis or B. licheniformis. In this study the response of B. pumilus to oxidative stress was investigated during a treatment with high concentrations of hydrogen peroxide at the proteome, transcriptome and metabolome level. Genes/proteins belonging to regulons, which are known to have important functions in the oxidative stress response of other organisms, were found to be upregulated, such as the Fur, Spx, SOS or CtsR regulon. Strikingly, parts of the fundamental PerR regulon responding to peroxide stress in B. subtilis are not encoded in the B. pumilus genome. Thus, B. pumilus misses the catalase KatA, the DNA-protection protein MrgA or the alkyl hydroperoxide reductase AhpCF. Data of this study suggests that the catalase KatX2 takes over the function of the missing KatA in the oxidative stress response of B. pumilus. The genome-wide expression analysis revealed an induction of bacillithiol (Cys-GlcN-malate, BSH) relevant genes. An analysis of the intracellular metabolites detected high intracellular levels of this protective metabolite, which indicates the importance of bacillithiol in the peroxide stress resistance of B. pumilus.
Y1  - 2014
U6  - http://dx.doi.org/10.1371/journal.pone.0085625
SN  - 1932-6203
VL  - 9
IS  - 1
PB  - PLOS
CY  - San Francisco
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  - Jakob, Felix
A1  - Martinez, Ronny
A1  - Mandawe, John
A1  - Hellmuth, Hendrik
A1  - Siegert, Petra
A1  - Maurer, Karl-Heinz
A1  - Schwaneberg, Ulrich
T1  - Surface charge engineering of a Bacillus gibsonii subtilisin protease
JF  - Applied microbiology and biotechnology
Y1  - 2013
SN  - 1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)
VL  - Vol. 97
IS  - Iss. 15
SP  - 6793
EP  - 6802
PB  - Springer
CY  - Berlin
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  - Martinez, Ronny
A1  - Jakob, Felix
A1  - Tu, Ran
A1  - Siegert, Petra
A1  - Maurer, Karl-Heinz
A1  - Schwaneberg, Ulrich
T1  - Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution
JF  - Biotechnology and bioengineering
Y1  - 2013
SN  - 1097-0290 (E-Journal); 0006-3592 (Print); 0368-1467 (Print)
VL  - Vol. 110
IS  - Iss. 3
SP  - 711
EP  - 720
PB  - Wiley
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Niehaus, F.
A1  - Gabor, E.
A1  - Wieland, S.
A1  - Siegert, Petra
A1  - Maurer, Karl-Heinz
A1  - Eck, J.
T1  - Enzymes for the laundry industries: tapping the vast metagenomic pool of alkaline proteases
JF  - Microbial biotechnology
Y1  - 2011
SN  - 1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)
VL  - Vol. 4
IS  - Iss. 6
SP  - 767
EP  - 776
PB  - Springer
CY  - Berlin
ER  -