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  - Molinnus, Denise
A1  - Muschallik, Lukas
A1  - Gonzalez, Laura Osorio
A1  - Bongaerts, Johannes
A1  - Wagner, Torsten
A1  - Selmer, Thorsten
A1  - Siegert, Petra
A1  - Keusgen, Michael
A1  - Schöning, Michael Josef
T1  - Development and characterization of a field-effect biosensor for the detection of acetoin
JF  - Biosensors and Bioelectronics
N2  - A capacitive electrolyte-insulator-semiconductor (EIS) field-effect biosensor for acetoin detection has been presented for the first time. The EIS sensor consists of a layer structure of Al/p-Si/SiO₂/Ta₂O₅/enzyme acetoin reductase. The enzyme, also referred to as butane-2,3-diol dehydrogenase from B. clausii DSM 8716T, has been recently characterized. The enzyme catalyzes the (R)-specific reduction of racemic acetoin to (R,R)- and meso-butane-2,3-diol, respectively. Two different enzyme immobilization strategies (cross-linking by using glutaraldehyde and adsorption) have been studied. Typical biosensor parameters such as optimal pH working range, sensitivity, hysteresis, linear concentration range and long-term stability have been examined by means of constant-capacitance (ConCap) mode measurements. Furthermore, preliminary experiments have been successfully carried out for the detection of acetoin in diluted white wine samples.
Y1  - 2018
U6  - http://dx.doi.org/10.1016/j.bios.2018.05.023
VL  - 115
SP  - 1
EP  - 6
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Bongaerts, Johannes
A1  - Esser, Simon
A1  - Lorbach, Volker
A1  - Al-Momani, Lóay
A1  - Müller, Michael A.
A1  - Franke, Dirk
A1  - Grondal, Christoph
A1  - Kurutsch, Anja
A1  - Bujnicki, Robert
A1  - Takors, Ralf
A1  - Raeven, Leon
A1  - Wubbolts, Marcel
A1  - Bovenberg, Roel
A1  - Nieger, Martin
A1  - Schürmann, Melanie
A1  - Trachtmann, Natalie
A1  - Kozak, Stefan
A1  - Sprenger, Georg A.
A1  - Müller, Michael
T1  - Diversity-oriented production of metabolites derived from chorismate and their use in organic synthesis
JF  - Angewandte Chemie International Edition
Y1  - 2011
SN  - 1521-3773 (E-Journal); 0570-0833 (Print); 1433-7851 (Print)
VL  - Vol. 50
IS  - Iss. 34
SP  - 7781
EP  - 7786
PB  - Wiley
CY  - Weinheim
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  - Borgmeier, Claudia
A1  - Bongaerts, Johannes
A1  - Meinhardt, Friedhelm
T1  - Genetic analysis of the Bacillus licheniformis degSU operon and the impact of regulatory mutations on protease production
JF  - Journal of biotechnology
N2  - Disruption experiments targeted at the Bacillus licheniformis degSU operon and GFP-reporter analysis provided evidence for promoter activity immediately upstream of degU. pMutin mediated concomitant introduction of the degU32 allele – known to cause hypersecretion in Bacillus subtilis – resulted in a marked increase in protease activity. Application of 5-fluorouracil based counterselection through establishment of a phosphoribosyltransferase deficient Δupp strain eventually facilitated the marker-free introduction of degU32 leading to further protease enhancement achieving levels as for hypersecreting wild strains in which degU was overexpressed. Surprisingly, deletion of rapG – known to interfere with DegU DNA-binding in B. subtilis – did not enhance protease production neither in the wild type nor in the degU32 strain. The combination of degU32 and Δupp counterselection in the type strain is not only equally effective as in hypersecreting wild strains with respect to protease production but furthermore facilitates genetic strain improvement aiming at biological containment and effectiveness of biotechnological processes.
KW  - Marker-free mutagenesis
KW  - Extracellular enzymes
KW  - Uracil-phosphoribosyltransferase
KW  - Hypersecretion
Y1  - 2012
U6  - http://dx.doi.org/10.1016/j.jbiotec.2012.02.011
SN  - 1873-4863 (E-Journal); 0168-1656 (Print)
VL  - 159
IS  - 1-2
SP  - 12
EP  - 20
PB  - Elsevier
CY  - Amsterdam
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  - 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  - Krämer, Marco
A1  - Bongaerts, Johannes
A1  - Bovenberg, Roel
A1  - Kremer, Susanne
A1  - Müller, Ulrike
A1  - Orf, Sonja
A1  - Wubbolts, Marcel
A1  - Raeven, Leon
T1  - Metabolic engineering for microbial production of shikimic acid
JF  - Metabolic engineering
Y1  - 2003
SN  - 1096-7184 (E-Journal); 1096-7176 (Print)
VL  - Vol. 5
IS  - Iss. 4
SP  - 277
EP  - 283
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  - Falkenberg, Fabian
A1  - Voß, Leonie
A1  - Bott, Michael
A1  - Bongaerts, Johannes
A1  - Siegert, Petra
T1  - New robust subtilisins from halotolerant and halophilic Bacillaceae
JF  - Applied Microbiology and Biotechnology
N2  - The aim of the present study was the characterisation of three true subtilisins and one phylogenetically intermediate subtilisin from halotolerant and halophilic microorganisms. Considering the currently growing enzyme market for efficient and novel biocatalysts, data mining is a promising source for novel, as yet uncharacterised enzymes, especially from halophilic or halotolerant Bacillaceae, which offer great potential to meet industrial needs. Both halophilic bacteria Pontibacillus marinus DSM 16465ᵀ and Alkalibacillus haloalkaliphilus DSM 5271ᵀ and both halotolerant bacteria Metabacillus indicus DSM 16189 and Litchfieldia alkalitelluris DSM 16976ᵀ served as a source for the four new subtilisins SPPM, SPAH, SPMI and SPLA. The protease genes were cloned and expressed in Bacillus subtilis DB104. Purification to apparent homogeneity was achieved by ethanol precipitation, desalting and ion-exchange chromatography. Enzyme activity could be observed between pH 5.0–12.0 with an optimum for SPPM, SPMI and SPLA around pH 9.0 and for SPAH at pH 10.0. The optimal temperature for SPMI and SPLA was 70 °C and for SPPM and SPAH 55 °C and 50 °C, respectively. All proteases showed high stability towards 5% (w/v) SDS and were active even at NaCl concentrations of 5 M. The four proteases demonstrate potential for future biotechnological applications.
KW  - Biotechnological application
KW  - Bacillaceae
KW  - Subtilisin
KW  - Subtilases
KW  - Halotolerant protease
Y1  - 2023
U6  - http://dx.doi.org/10.1007/s00253-023-12553-w
SN  - 1432-0614
N1  - Corresponding author: Petra Siegert
VL  - 107
SP  - 3939
EP  - 3954
PB  - Springer Nature
CY  - Berlin
ER  -