TY  - INPR
A1  - Greiner, Lasse
A1  - Jeromin, Günter Erich
A1  - Sithole, Patience
A1  - Petersen, Soenke
T1  - Preprint: Studies on the enzymatic reduction of levulinic acid using Chiralidon-R and Chiralidon-S
T2  - ChemRxiv
N2  - The enzymatic reduction of levulinic acid by the chiral catalysts Chiralidon-R and Chiralidon-S which are commercially available superabsorbed alcohol dehydrogenases is described. The Chiralidon®-R/S reduces the levulinic acid to the (R,S)-4-hydroxy valeric acid and the (R)- or (S)- gamma-valerolactone.
KW  - Levulinic acid
KW  - Chiralidon-R
KW  - Chiralidon-S
KW  - 4-hydroxy valeric acid
KW  - (R)- or (S)- gamma-valerolactone
Y1  - 2023
U6  - https://doi.org/10.26434/chemrxiv-2023-jlvcv
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  - https://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  - Muschallik, Lukas
A1  - Molinnus, Denise
A1  - Bongaerts, Johannes
A1  - Pohl, Martina
A1  - Wagner, Torsten
A1  - Schöning, Michael Josef
A1  - Siegert, Petra
A1  - Selmer, Thorsten
T1  - (R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme
JF  - Journal of Biotechnology
N2  - The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33–43%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.
Y1  - 2017
U6  - https://doi.org/10.1016/j.jbiotec.2017.07.020
SN  - 0168-1656
VL  - 258
SP  - 41
EP  - 50
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Jossek, Ralf
A1  - Bongaerts, Johannes
A1  - Sprenger, Georg A.
T1  - Characterization of a new feedback-resistant 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase AroF of Escherichia coli
JF  - FEMS microbiology letters
Y1  - 2001
SN  - 1574-6968
VL  - Vol. 202
IS  - Iss. 1
SP  - 145
EP  - 148
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  - Seifarth, Volker
A1  - Grosse, Joachim O.
A1  - Grossmann, Matthias
A1  - Janke, Heinz Peter
A1  - Arndt, Patrick
A1  - Koch, Sabine
A1  - Epple, Matthias
A1  - Artmann, Gerhard
A1  - Temiz Artmann, Aysegül
T1  - Mechanical induction of bi-directional orientation of primary porcine bladder smooth muscle cells in tubular fibrin-poly(vinylidene fluoride) scaffolds for ureteral and urethral repair using cyclic and focal balloon catheter stimulation
JF  - Journal of Biomaterials Applications
Y1  - 2017
U6  - https://doi.org/10.1177/0885328217723178
SN  - 1530-8022
VL  - 32
IS  - 3
SP  - 321
EP  - 330
PB  - Sage
CY  - London
ER  - 
TY  - JOUR
A1  - Seifarth, Volker
A1  - Goßmann, Matthias
A1  - Grosse, J. O.
A1  - Becker, C.
A1  - Heschel, I.
A1  - Artmann, Gerhard
A1  - Temiz Artmann, Aysegül
T1  - Development of a Bioreactor to Culture Tissue Engineered Ureters Based on the Application of Tubular OPTIMAIX 3D Scaffolds
JF  - Urologia Internationalis
Y1  - 2015
U6  - https://doi.org/10.1159/000368419
SN  - 0042-1138
VL  - 2015
IS  - 95
SP  - 106
EP  - 113
PB  - Karger
CY  - Basel
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  - 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  - https://doi.org/10.1016/j.bios.2018.05.023
VL  - 115
SP  - 1
EP  - 6
PB  - Elsevier
CY  - Amsterdam
ER  -