Naslov
Different strategies for multi-enzyme cascade reaction for chiral vic-1,2-diol production

Autori
Vrsalović Presečki, Ana ; Pintarić, Lela ; Švarc, Anera ; Vasić-Rački, Đurđa

Izvornik
Bioprocess and biosystems engineering (1615-7591) 41 (2018), 6; 793-802

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
multi-enzyme cascade reaction ; asymmetric reduction ; stereoselectivity ; alcohol dehydrogenase ; benzoylformate decarboxylase

Sažetak
The stereoselective three-enzyme cascade for the one-pot synthesis of (1S, 2S)-1- phenylpropane-1, 2-diol ((1S, 2S)-1-PPD) from inexpensive starting substrates, benzaldehyde and acetaldehyde, was explored. By coupling stereoselective carboligation catalyzed by benzoylformate decarboxylase (BFD), L-selective reduction of a carbonyl group with alcohol dehydrogenase from Lactobacillus brevis (ADHLb) as well as the coenzyme regeneration by formate dehydrogenase (FDH), enantiomerically pure diastereoselective 1, 2-diol was produced. Two different multi-enzyme system approaches were applied: the sequential two-step one-pot and the simultaneous one-pot cascade. All enzymes were kinetically characterized. The impact of acetal-dehyde on the BFD and ADHLb stability was investigated. To overcome the kinetic limitation of acetaldehyde in the carbo- ligation reaction and to reduce its influence on the enzyme stability, experiments were performed in two different excesses of acetaldehyde (100 and 300%). Due to the ADHLb deactivation by acetaldehyde, the simultaneous one-pot cascade proved not to be the first choice for the investigated three-enzyme system. In the sequential cascade with 300% acetaldehyde excess a 100% yield of vic 1, 2- diol was reached.

Izvorni jezik
Engleski

Znanstvena područja
Kemijsko inženjerstvo, Biotehnologija

POVEZANOST RADA