Pregled bibliografske jedinice broj: 694119
Mathematical modeling of (S)-2-hydroxypropiophenone reduction to optically active diols catalyzed by alcohol and glycerol dehydrogenase
Mathematical modeling of (S)-2-hydroxypropiophenone reduction to optically active diols catalyzed by alcohol and glycerol dehydrogenase // 3rd Multistep Enzyme Catalyzed Processes Congress (MECP14)
Madrid, Španjolska, 2014. (poster, nije recenziran, neobjavljeni rad, znanstveni)
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Naslov
Mathematical modeling of (S)-2-hydroxypropiophenone reduction to optically active diols catalyzed by alcohol and glycerol dehydrogenase
Autori
Valinger, Davor ; Vrsalović Presečki, Ana ; Vasić-Rački, Đurđa ; Kurtanjek Želimir
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, neobjavljeni rad, znanstveni
Skup
3rd Multistep Enzyme Catalyzed Processes Congress (MECP14)
Mjesto i datum
Madrid, Španjolska, 07.04.2014. - 10.04.2014
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
(S)-2-hydroxypropiophenone; optically active diols
Sažetak
(S)-2-hydroxypropiophenone ((S)-2-HPP) is the product of carboligaton reaction of benyaldehyde and acetaldehyde catalyzed by benzoylformate decarboxylase from Pseudomonas putida. In this study reduction of (S)-2-HPP to (1R, 2S)-1-phenylpropane-1, 2-diol catalyzed by alcohol dehydrogenase (ADH) from Lactobacillus brevis (LbADH) and (1S, 2S)-1-phenylpropane-1, 2-diol catalyzed by glycerol dehydrogenase (GDH) from Cellulomonas sp. was investigated. ADH and GDH are enzymes that require coenzyme NAD+(H) for its action. The regeneration of coenzyme NADH was performed by using a second enzyme, the formate dehydrogenase from Candida boidinii (FDH) that catalyzes the reaction of formate oxidation. The kinetics of all reactions was determined by using the initial reaction rates method. Based on the kinetic results mathematical model was developed and was validated in batch reactor for production of both dioles in the system with and without regeneration of NADH coenzyme. In the systems without regeneration the equilibrium conversion of 60 % was achieved for the (S)-2-HPP reduction catalyzed by ADH, while for the same reaction catalyzed by GDH the conversion was 34 %. The reactions catalyzed by both enzymes in the system with coenzyme regeneration by FDH resulted with the S-(2)-HPP conversion of 100 %.
Izvorni jezik
Engleski
Znanstvena područja
Kemijsko inženjerstvo, Biotehnologija
POVEZANOST RADA
Ustanove:
Prehrambeno-biotehnološki fakultet, Zagreb,
Fakultet kemijskog inženjerstva i tehnologije, Zagreb
Profili:
Davor Valinger
(autor)
Želimir Kurtanjek
(autor)
Ana Vrsalović Presečki
(autor)
Đurđa Vasić-Rački
(autor)