Pregled bibliografske jedinice broj: 886399
OPTIMIZATION OF ENZYME CATALYZED ALDOL ADDITION OF PROPANAL AND FORMALDEHYDE
OPTIMIZATION OF ENZYME CATALYZED ALDOL ADDITION OF PROPANAL AND FORMALDEHYDE // Biotrans 2017, 13th International Symposium on Biocatalysis and Biotransformations
Budimpešta, Mađarska, 2017. str. P-037 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 886399 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
OPTIMIZATION OF ENZYME CATALYZED ALDOL ADDITION OF PROPANAL AND FORMALDEHYDE
Autori
Findrik Blažević, Zvjezdana ; Česnik, Morana ; Vasić-Rački, Đurđa ; Hernández, Karel, Clapés, Pere
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Biotrans 2017, 13th International Symposium on Biocatalysis and Biotransformations
/ - , 2017, P-037
Skup
Biotrans 2017, 13th International Symposium on Biocatalysis and Biotransformations
Mjesto i datum
Budimpešta, Mađarska, 09.07.2017. - 13.07.2017
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
aldol addition, FSA, optimization, mathematical modeling
Sažetak
Carbon-carbon bond formation is the essence of organic synthesis and provides the foundation for generating more complex compounds from the simpler ones.[1] Aldolases catalyze the reversible carbon–carbon bond formation by aldol addition of a nucleophilic donor to an electrophilic aldehyde acceptor.[2] In this work aldol addition of formaldehyde and propanal catalyzed by D-fructose-6-phosphate aldolase (FSA) was investigated (Fig 1). This reaction has not been studied up to now. Figure 1. Reaction scheme of aldol addition between formaldehyde and propanal catalyzed by FSA. The main focus was put on the kinetic model development, finding the best reactor mode and process conditions to obtain the maximum concentration of aldol product and ensure the best use of enzyme. Thus, kinetic analysis of the reaction system was done and the reaction rate was described by the two substrate Michaelis-Menten kinetic model with included inhibitions by both substrates. It was found that propanal is very reactive at reaction conditions and causes formation of side- products with and without the presence of enzyme. Thus, the kinetics of side-reactions were also investigated to ensure good applicability of the mathematical model, and to try minimizing the formation of side-products. Enzyme operational stability was also experimentally evaluated. The model was validated in the batch reactor. By combining the kinetic model for the enzymatic aldol addition, as well as for side-reactions that occur, with mass balances in batch and fed- batch reactor, simulations were done to find the optimal conditions for this reaction system. [1] Li, C.-J. Chem. Rev. 2005, 105, 3095- 3165. [2] Clapés, P. ; Fessner, W.-D. ; Sprenger, G.A. ; Samland, A.K. Curr. Opin. Chem. Biol. 2010, 14, 154–167. Project CARBAZYMES-This project has received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 635595.
Izvorni jezik
Engleski
Znanstvena područja
Kemijsko inženjerstvo, Biotehnologija
Napomena
Project CARBAZYMES-This project has received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 635595.
POVEZANOST RADA
Ustanove:
Fakultet kemijskog inženjerstva i tehnologije, Zagreb