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Author

  • Johannes Bongaerts (5)
  • Lukas Muschallik (5)
  • Michael J. Schöning (5)
  • Petra Siegert (5)
  • Denise Molinnus (4)
  • Thorsten Selmer (4)
  • Torsten Wagner (4)
  • Martina Pohl (3)
  • Carina Ronja Kipp (2)
  • Melanie Jablonski (2)
  • Michael Keusgen (2)
  • Felix Münstermann (1)
  • Inga Recker (1)
  • Jasmina Nork (1)
  • Laura Osorio Gonzalez (1)
  • Melanie Gelissen (1)

Year of publication

  • 2021 (1)
  • 2020 (2)
  • 2018 (1)
  • 2017 (1)

Keywords

  • acetoin (1)
  • acetoin reductase (1)
  • alcoholic beverages (1)
  • biosensors (1)
  • capacitive field-effect sensors (1)

Institute

  • Fachbereich Chemie und Biotechnologie (5)
  • Fachbereich Medizintechnik und Technomathematik (5)
  • INB - Institut für Nano- und Biotechnologien (5)

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(R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme (2017)
Lukas Muschallik ; Denise Molinnus ; Johannes Bongaerts ; Martina Pohl ; Torsten Wagner ; Michael J. Schöning ; Petra Siegert ; Thorsten Selmer
Synthesis of α-hydroxy ketones and vicinal diols with the Bacillus licheniformis DSM 13T butane-2, 3-diol dehydrogenase (2020)
Lukas Muschallik ; Carina Ronja Kipp ; Inga Recker ; Johannes Bongaerts ; Martina Pohl ; Melanie Gelissen ; Michael J. Schöning ; Thorsten Selmer ; Petra Siegert
The enantioselective synthesis of α-hydroxy ketones and vicinal diols is an intriguing field because of the broad applicability of these molecules. Although, butandiol dehydrogenases are known to play a key role in the production of 2,3-butandiol, their potential as biocatalysts is still not well studied. Here, we investigate the biocatalytic properties of the meso-butanediol dehydrogenase from Bacillus licheniformis DSM 13T (BlBDH). The encoding gene was cloned with an N-terminal StrepII-tag and recombinantly overexpressed in E. coli. BlBDH is highly active towards several non-physiological diketones and α-hydroxyketones with varying aliphatic chain lengths or even containing phenyl moieties. By adjusting the reaction parameters in biotransformations the formation of either the α-hydroxyketone intermediate or the diol can be controlled.
Synthesis of α-hydroxy ketones and vicinal (R, R)-diols by Bacillus clausii DSM 8716ᵀ butanediol dehydrogenase (2020)
Lukas Muschallik ; Denise Molinnus ; Melanie Jablonski ; Carina Ronja Kipp ; Johannes Bongaerts ; Martina Pohl ; Torsten Wagner ; Michael J. Schöning ; Thorsten Selmer ; Petra Siegert
α-hydroxy ketones (HK) and 1,2-diols are important building blocks for fine chemical synthesis. Here, we describe the R-selective 2,3-butanediol dehydrogenase from B. clausii DSM 8716ᵀ (BcBDH) that belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR) and catalyzes the selective asymmetric reduction of prochiral 1,2-diketones to the corresponding HK and, in some cases, the reduction of the same to the corresponding 1,2-diols. Aliphatic diketones, like 2,3-pentanedione, 2,3-hexanedione, 5-methyl-2,3-hexanedione, 3,4-hexanedione and 2,3-heptanedione are well transformed. In addition, surprisingly alkyl phenyl dicarbonyls, like 2-hydroxy-1-phenylpropan-1-one and phenylglyoxal are accepted, whereas their derivatives with two phenyl groups are not substrates. Supplementation of Mn²⁺ (1 mM) increases BcBDH's activity in biotransformations. Furthermore, the biocatalytic reduction of 5-methyl-2,3-hexanedione to mainly 5-methyl-3-hydroxy-2-hexanone with only small amounts of 5-methyl-2-hydroxy-3-hexanone within an enzyme membrane reactor is demonstrated.
Development and characterization of a field-effect biosensor for the detection of acetoin (2018)
Denise Molinnus ; Lukas Muschallik ; Laura Osorio Gonzalez ; Johannes Bongaerts ; Torsten Wagner ; Thorsten Selmer ; Petra Siegert ; Michael Keusgen ; Michael J. Schöning
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.
Capacitive field‐effect biosensor applied for the detection of acetoin in alcoholic beverages and fermentation broths (2021)
Melanie Jablonski ; Felix Münstermann ; Jasmina Nork ; Denise Molinnus ; Lukas Muschallik ; Johannes Bongaerts ; Torsten Wagner ; Michael Keusgen ; Petra Siegert ; Michael J. Schöning
An acetoin biosensor based on a capacitive electrolyte–insulator–semiconductor (EIS) structure modified with the enzyme acetoin reductase, also known as butane-2,3-diol dehydrogenase (Bacillus clausii DSM 8716ᵀ), is applied for acetoin detection in beer, red wine, and fermentation broth samples for the first time. The EIS sensor consists of an Al/p-Si/SiO₂/Ta₂O₅ layer structure with immobilized acetoin reductase on top of the Ta₂O₅ transducer layer by means of crosslinking via glutaraldehyde. The unmodified and enzyme-modified sensors are electrochemically characterized by means of leakage current, capacitance–voltage, and constant capacitance methods, respectively.
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