Pregled bibliografske jedinice broj: 195527
Kinetic modeling of acetophenone reduction catalyzed by alcohol dehydrogenase from Thermoanaerobacter sp.
Kinetic modeling of acetophenone reduction catalyzed by alcohol dehydrogenase from Thermoanaerobacter sp. // Biotechnology letters, 27 (2005), 15; 1087-1095 doi:10.1007/s10529-005-8455-y (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 195527 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Kinetic modeling of acetophenone reduction catalyzed by alcohol dehydrogenase from Thermoanaerobacter sp.
Autori
Findrik, Zvjezdana ; Vasić-Rački, Đurđa ; Lütz, Stephan ; Daußmann, Thomas ; Wandrey, Christian
Izvornik
Biotechnology letters (0141-5492) 27
(2005), 15;
1087-1095
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
alcohol dehydrogenase ; cofactor regeneration ; enzyme deactivation ; enzyme kinetics
Sažetak
NADPH-dependent alcohol dehydrogenase (ADH) from Thermoanaerobacter sp. was kinetically characterized using reduction of acetophenone as a model. To achieve 98 % conversion of acetophenone, cofactor regeneration by oxidation of 2-propanol with the same enzyme was used. The enzyme was stable in the batch reactor. It showed to be highly enantioselective towards (S)-1- phenylethanol (ee > 99.5 %). Due to its high deactivation in continuously operated stirred tank reactor (kd = 0.0141 min-1) there was no way to keep high conversion of acetophenone at 98 %. The deactivation occurred in the repetitive batch as well. A mathematical model for the acetophenone reduction with cofactor regeneration describing the behaviour in a batch, repetitive-batch and continuously stirred tank reactor was developed.
Izvorni jezik
Engleski
Znanstvena područja
Kemijsko inženjerstvo, Biotehnologija
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE
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