Details
| Original language | English |
|---|---|
| Pages (from-to) | 24-28 |
| Number of pages | 5 |
| Journal | Journal of Molecular Catalysis B: Enzymatic |
| Volume | 103 |
| Early online date | 1 Dec 2013 |
| Publication status | Published - May 2014 |
| Externally published | Yes |
Abstract
Alcohol dehydrogenases form one of the most important enzyme classes for the synthesis of chiral hydroxyl-compounds. High solvent concentrations may improve the efficiency of biocatalytic ADH reactions but, however, turned out to damage most enzymes. In order to overcome the damage caused to these enzymes, this work describes the stabilization of five different alcohol dehydrogenases under very high solvent concentrations (up to 90% of the reaction volume). The reductive conversion of the ketone substrate into the corresponding alcohol was increased up to sevenfold by pre-incubating the enzymes with specific stabilizers. This technique is highly efficient and additionally facile as no prior immobilization, polymerization or deposition treatment is necessary. It was revealed that each ADH gained an optimal stabilization effect by one specific stabilizer and appropriate concentration. Furthermore, the results obtained on laboratory scale were transferred successfully to 4000 mL scale to verify the applicability of this technique for industrial use.
Keywords
- Additives, ADH, Industry, Stabilization
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemical Engineering(all)
- Bioengineering
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Chemical Engineering(all)
- Process Chemistry and Technology
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Journal of Molecular Catalysis B: Enzymatic, Vol. 103, 05.2014, p. 24-28.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Alcohol dehydrogenase stabilization by additives under industrially relevant reaction conditions
AU - Spickermann, Dominik
AU - Kara, Selin
AU - Barackov, Ivana
AU - Hollmann, Frank
AU - Schwaneberg, Ulrich
AU - Duenkelmann, Pascal
AU - Leggewie, Christian
N1 - Funding Information: The authors thank Deutsche Bundesstiftung Umwelt (DBU) for financial support of the project (AZ 13261). David Hopkins, Marion Lammertz and Stefanie Kind are acknowledged for fruitful discussions and theoretical input.
PY - 2014/5
Y1 - 2014/5
N2 - Alcohol dehydrogenases form one of the most important enzyme classes for the synthesis of chiral hydroxyl-compounds. High solvent concentrations may improve the efficiency of biocatalytic ADH reactions but, however, turned out to damage most enzymes. In order to overcome the damage caused to these enzymes, this work describes the stabilization of five different alcohol dehydrogenases under very high solvent concentrations (up to 90% of the reaction volume). The reductive conversion of the ketone substrate into the corresponding alcohol was increased up to sevenfold by pre-incubating the enzymes with specific stabilizers. This technique is highly efficient and additionally facile as no prior immobilization, polymerization or deposition treatment is necessary. It was revealed that each ADH gained an optimal stabilization effect by one specific stabilizer and appropriate concentration. Furthermore, the results obtained on laboratory scale were transferred successfully to 4000 mL scale to verify the applicability of this technique for industrial use.
AB - Alcohol dehydrogenases form one of the most important enzyme classes for the synthesis of chiral hydroxyl-compounds. High solvent concentrations may improve the efficiency of biocatalytic ADH reactions but, however, turned out to damage most enzymes. In order to overcome the damage caused to these enzymes, this work describes the stabilization of five different alcohol dehydrogenases under very high solvent concentrations (up to 90% of the reaction volume). The reductive conversion of the ketone substrate into the corresponding alcohol was increased up to sevenfold by pre-incubating the enzymes with specific stabilizers. This technique is highly efficient and additionally facile as no prior immobilization, polymerization or deposition treatment is necessary. It was revealed that each ADH gained an optimal stabilization effect by one specific stabilizer and appropriate concentration. Furthermore, the results obtained on laboratory scale were transferred successfully to 4000 mL scale to verify the applicability of this technique for industrial use.
KW - Additives
KW - ADH
KW - Industry
KW - Stabilization
UR - http://www.scopus.com/inward/record.url?scp=84895175075&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2013.11.015
DO - 10.1016/j.molcatb.2013.11.015
M3 - Article
AN - SCOPUS:84895175075
VL - 103
SP - 24
EP - 28
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
SN - 1381-1177
ER -