TY  - PAT
A1  - Wieland, Susanne
A1  - Siegert, Petra
A1  - Spitz, Astrid
A1  - Maurer, Karl-Heinz
A1  - O'Connell, Timothy
A1  - Prüser, Inken
A1  - Schiedel, Marc-Steffen
A1  - Eiting, Thomas
A1  - Sendor-Müller, Dorota
A1  - Bastigkeit, Thorsten
A1  - Benda, Konstantin
A1  - Müller, Sven
T1  - Lagerstabiles flüssiges Wasch- oder Reinigungsmittel enthaltend Proteasen [Offenlegungsschrift]
T1  - Storage-stable liquid washing or cleaning agent containing proteases [Europäische Patentanmeldung / Internationale Patentanmeldung]
Y1  - 2011
SP  - 1
EP  - 25
PB  - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO
CY  - München / Den Hague / Genf
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  - 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  - 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  - PAT
A1  - Maurer, Karl-Heinz
A1  - O'Connell, Timothy
A1  - Siegert, Petra
A1  - Weber, Thomas
A1  - Tondera, Susanne
A1  - Hellmuth, Hendrik
T1  - Flüssige Tensidzubereitung enthaltend Lipase und Phosphonat [Offenlegungsschrift]
T1  - Liquid surfactant preparation containing lipase and phosphonate [Europäische Patentanmeldung / Internationale Patentanmeldung]
Y1  - 2012
SP  - 1
EP  - 22
PB  - Deutsches Patent- und Markenamt / Europäisches Patentamt / WIPO
CY  - München / Den Hague / Genf
ER  - 
TY  - JOUR
A1  - Ribitsch, D.
A1  - Heumann, S.
A1  - Karl, W.
A1  - Gerlach, J.
A1  - Leber, R.
A1  - Birner-Gruenberger, R.
A1  - Gruber, K.
A1  - Eiteljoerg, I.
A1  - Remler, P.
A1  - Siegert, Petra
A1  - Lange, J.
A1  - Maurer, Karl-Heinz
A1  - Berg, G.
A1  - Guebitz, G. M.
A1  - Schwab, H.
T1  - Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli
JF  - Journal of biotechnology
N2  - A large strain collection comprising antagonistic bacteria was screened for novel detergent proteases. Several strains displayed protease activity on agar plates containing skim milk but were inactive in liquid media. Encapsulation of cells in alginate beads induced protease production. Stenotrophomonas maltophilia emerged as best performer under washing conditions. For identification of wash-active proteases, four extracellular serine proteases called StmPr1, StmPr2, StmPr3 and StmPr4 were cloned. StmPr2 and StmPr4 were sufficiently overexpressed in E. coli. Expression of StmPr1 and StmPr3 resulted in unprocessed, insoluble protein. Truncation of most of the C-terminal domain which has been identified by enzyme modeling succeeded in expression of soluble, active StmPr1 but failed in case of StmPr3.

From laundry application tests StmPr2 turned out to be a highly wash-active protease at 45 °C. Specific activity of StmPr2 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 17 ± 2 U/mg. In addition we determined the kinetic parameters and cleavage preferences of protease StmPr2.
KW  - Alginate beads
KW  - Stenotrophomonas maltophilia
KW  - Detergent protease
Y1  - 2012
U6  - http://dx.doi.org/10.1016/j.jbiotec.2011.09.025
SN  - 1873-4863 (E-Journal); 0168-1656 (Print)
VL  - 157
IS  - 1
SP  - 140
EP  - 147
PB  - Elsevier
CY  - Amsterdam
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  - 
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  - 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  -