TY  - JOUR
A1  - Pohl, Martina
A1  - Siegert, Petra
A1  - Mesch, K.
A1  - Bruhn, H.
A1  - Grötzinger, Joachim
T1  - Active site mutants of pyruvate decarboxylase from Zymomonas mobilis : a site-directed mutagenesis study of L112, I472, I476, E473 and N482
JF  - European journal of biochemistry
Y1  - 1998
SN  - 1432-1033 (E-Journal); 1742-4658 (E-Journal); 0014-2956 (Print); 1742-464X (Print)
VL  - Vol. 257
IS  - Iss. 3
SP  - 538
EP  - 546
ER  - 
TY  - RPRT
A1  - Haeger, Gerrit
A1  - Bongaerts, Johannes
A1  - Siegert, Petra
T1  - Abschlussbericht Teil II: Eingehende Darstellung Neue biobasierte Lipopeptide aus nachhaltiger Produktion (LipoPep)
Y1  - 2023
N1  - Förderkennzeichen: 13FH256PA6

Titel: FHprofUnt 2016: Neue biobasierte Lipopeptide aus nachhaltiger Produktion

Laufzeit: 01.02.2019 – 31.10.2022
ER  - 
TY  - JOUR
A1  - Haeger, Gerrit
A1  - Bongaerts, Johannes
A1  - Siegert, Petra
T1  - A convenient ninhydrin assay in 96-well format for amino acid-releasing enzymes using an air-stable reagent
JF  - Analytical Biochemistry
N2  - An improved and convenient ninhydrin assay for aminoacylase activity measurements was developed using the commercial EZ Nin™ reagent. Alternative reagents from literature were also evaluated and compared. The addition of DMSO to the reagent enhanced the solubility of Ruhemann's purple (RP). Furthermore, we found that the use of a basic, aqueous buffer enhances stability of RP. An acidic protocol for the quantification of lysine was developed by addition of glacial acetic acid. The assay allows for parallel processing in a 96-well format with measurements microtiter plates.
Y1  - 2022
U6  - http://dx.doi.org/10.1016/j.ab.2022.114819
SN  - 1096-0309
IS  - 624
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - PAT
A1  - Banowski, Bernhard
A1  - Waldmann-Laue, Marianne
A1  - Wadle, Armin
A1  - Siegert, Petra
A1  - Sättler, Andreas
T1  - 5-Lipoxigenase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift]
T1  - 5-Lipooxygenase inhibitors in deodorants and antiperspirants [Europäische Patentanmeldung]
Y1  - 2004
SP  - 1
EP  - 12
PB  - Deutsches Patent- und Markenamt / Europäisches Patentamt
CY  - München / Den Hague
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  - http://dx.doi.org/10.1016/j.jbiotec.2017.07.020
SN  - 0168-1656
VL  - 258
SP  - 41
EP  - 50
PB  - Elsevier
CY  - Amsterdam
ER  -