Pregled bibliografske jedinice broj: 639312
Aldol addition of dihydroxyacetone to N-Cbz-3- aminopropanal catalyzed by two different D- fructose-6-phosphate aldolases
Aldol addition of dihydroxyacetone to N-Cbz-3- aminopropanal catalyzed by two different D- fructose-6-phosphate aldolases // Biotrans 2013 delegate book / Turner, Nicholas (ur.).
Manchester, 2013. str. 80-80 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 639312 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Aldol addition of dihydroxyacetone to N-Cbz-3- aminopropanal catalyzed by two different D- fructose-6-phosphate aldolases
Autori
Sudar, Martina ; Findrik Blažević, Zvjezdana ; Vasić- Rački, Đurđa ; Clapes, Pere
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Biotrans 2013 delegate book
/ Turner, Nicholas - Manchester, 2013, 80-80
Skup
Biotrans 2013
Mjesto i datum
Manchester, Ujedinjeno Kraljevstvo, 21.07.2013. - 25.07.2013
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
aldolase; aldol addition; enzyme kinetics; microreactor
Sažetak
Aldolases belong to a group of enzymes called lyases and they catalyze carbon-carbon bond formation [1]. In this work aldol addition of dihydroxyacetone (DHA) to N-Cbz-3-aminopropanal (aldehyde) was studied. The aldol product of the reaction is used as precursor in the production of D-fagomine, a naturally occurring iminosugar with remarkable biological properties [2]. The reaction was catalyzed by D-fructose-6-phosphate aldolase overexpressed in E. coli. Two different aldolases were investigated, FSA A129S and FSA A129S/A165G. The dependence of enzyme activity on pH was measured for these two enzymes. Furthermore, since aldehyde is not soluble in water, two different co-solvents (acetonitrile and dimethylformamide) were selected and the influence of these co- solvents and their volume percentage in the reaction mixture on the enzyme activity was studied using the initial reaction rate method. Enzyme kinetics was determined in the batch reactor and kinetic parameters of enzymes were compared. Aldol addition catalyzed by the two enzymes was carried out in the microreactor. Enzyme activity was followed during the experiments. References: [1] Lopez-Santin et al, Illanes ed., Springer, 2008, 333 – 352 [2] Castillo et al, Org. Lett. 2006, 8, 6067-6070.
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija
POVEZANOST RADA
Projekti:
125-1252086-2793 - Biokatalizatori i biotransformacije (Vasić-Rački, Đurđa, MZOS ) ( CroRIS)
Ustanove:
Fakultet kemijskog inženjerstva i tehnologije, Zagreb