Details
| Original language | English |
|---|---|
| Pages (from-to) | 973-976 |
| Number of pages | 4 |
| Journal | CHEMCATCHEM |
| Volume | 6 |
| Issue number | 4 |
| Early online date | 12 Feb 2014 |
| Publication status | Published - 10 Apr 2014 |
| Externally published | Yes |
Abstract
Highly productive biocatalytic reductions were established using an isolated alcohol dehydrogenase (ADH) under water-deficient conditions. First, a solvent-free system was evaluated for the reduction of 2-butanone catalyzed by ADH evo-1.1.200 promoted by the "smart cosubstrate" 1,4-butanediol. ADH evo-1.1.200 excelled by its activity and stability under high reagent concentrations and hence was the enzyme of choice. However, conversion of 2-butanone was limited to <1 % in 10 days under the solvent-free conditions. Therefore, water-immiscible organic solvents were evaluated whereby the highest conversions were achieved in MTBE and toluene. MTBE was chosen as its different boiling point compared to other reaction components (e.g., 2-butanone, 2-butanol, diol cosubstrate, and lactone coproduct) would simplify the downstream processing. Further on, by tuning substrate loading, the productivity of the ADH evo-1.1.200 was successfully increased to a turnover number (TON) of 64 000. Practical water-deficient enzymology for bioreductions: The use of alcohol dehydrogenases (ADHs) in neat substrates and in water-immiscible organic solvents is explored. The ADH evo-1.1.200 excelled by its high stability, as it showed significant catalytic activity over days. Reductions are coupled with the "smart cosubstrate" 1,4-butanediol; hence, excess amounts of reductants are avoided.
Keywords
- alcohol dehydrogenases, biotransformations, organic media, reduction, smart cosubstrates
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemistry(all)
- Physical and Theoretical Chemistry
- Chemistry(all)
- Organic Chemistry
- Chemistry(all)
- Inorganic Chemistry
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In: CHEMCATCHEM, Vol. 6, No. 4, 10.04.2014, p. 973-976.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Bioreductions catalyzed by an alcohol dehydrogenase in non-aqueous media
AU - Kara, Selin
AU - Spickermann, Dominik
AU - Weckbecker, Andrea
AU - Leggewie, Christian
AU - Arends, Isabel W.C.E.
AU - Hollmann, Frank
PY - 2014/4/10
Y1 - 2014/4/10
N2 - Highly productive biocatalytic reductions were established using an isolated alcohol dehydrogenase (ADH) under water-deficient conditions. First, a solvent-free system was evaluated for the reduction of 2-butanone catalyzed by ADH evo-1.1.200 promoted by the "smart cosubstrate" 1,4-butanediol. ADH evo-1.1.200 excelled by its activity and stability under high reagent concentrations and hence was the enzyme of choice. However, conversion of 2-butanone was limited to <1 % in 10 days under the solvent-free conditions. Therefore, water-immiscible organic solvents were evaluated whereby the highest conversions were achieved in MTBE and toluene. MTBE was chosen as its different boiling point compared to other reaction components (e.g., 2-butanone, 2-butanol, diol cosubstrate, and lactone coproduct) would simplify the downstream processing. Further on, by tuning substrate loading, the productivity of the ADH evo-1.1.200 was successfully increased to a turnover number (TON) of 64 000. Practical water-deficient enzymology for bioreductions: The use of alcohol dehydrogenases (ADHs) in neat substrates and in water-immiscible organic solvents is explored. The ADH evo-1.1.200 excelled by its high stability, as it showed significant catalytic activity over days. Reductions are coupled with the "smart cosubstrate" 1,4-butanediol; hence, excess amounts of reductants are avoided.
AB - Highly productive biocatalytic reductions were established using an isolated alcohol dehydrogenase (ADH) under water-deficient conditions. First, a solvent-free system was evaluated for the reduction of 2-butanone catalyzed by ADH evo-1.1.200 promoted by the "smart cosubstrate" 1,4-butanediol. ADH evo-1.1.200 excelled by its activity and stability under high reagent concentrations and hence was the enzyme of choice. However, conversion of 2-butanone was limited to <1 % in 10 days under the solvent-free conditions. Therefore, water-immiscible organic solvents were evaluated whereby the highest conversions were achieved in MTBE and toluene. MTBE was chosen as its different boiling point compared to other reaction components (e.g., 2-butanone, 2-butanol, diol cosubstrate, and lactone coproduct) would simplify the downstream processing. Further on, by tuning substrate loading, the productivity of the ADH evo-1.1.200 was successfully increased to a turnover number (TON) of 64 000. Practical water-deficient enzymology for bioreductions: The use of alcohol dehydrogenases (ADHs) in neat substrates and in water-immiscible organic solvents is explored. The ADH evo-1.1.200 excelled by its high stability, as it showed significant catalytic activity over days. Reductions are coupled with the "smart cosubstrate" 1,4-butanediol; hence, excess amounts of reductants are avoided.
KW - alcohol dehydrogenases
KW - biotransformations
KW - organic media
KW - reduction
KW - smart cosubstrates
UR - http://www.scopus.com/inward/record.url?scp=84898655052&partnerID=8YFLogxK
U2 - 10.1002/cctc.201300841
DO - 10.1002/cctc.201300841
M3 - Article
AN - SCOPUS:84898655052
VL - 6
SP - 973
EP - 976
JO - CHEMCATCHEM
JF - CHEMCATCHEM
SN - 1867-3880
IS - 4
ER -