Pregled bibliografske jedinice broj: 886864
Enzymatic cascade reaction for the synthesis of imino sugar precursors
Enzymatic cascade reaction for the synthesis of imino sugar precursors // Book of Abstracts
Budimpešta: Hungarian Chemical Society, 2017. str. 100-100 (poster, nije recenziran, sažetak, znanstveni)
CROSBI ID: 886864 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Enzymatic cascade reaction for the synthesis of imino sugar precursors
Autori
Česnik, Morana ; Sudar, Martina ; Vasić-Rački, Đurđa ; Clapés, Pere ; Findrik Blažević, Zvjezdana
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Book of Abstracts
/ - Budimpešta : Hungarian Chemical Society, 2017, 100-100
ISBN
978-963-9970-76-2
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
Nije recenziran
Ključne riječi
enzymatic cascade reactions, imino sugars, aldol addition
Sažetak
Multistep enzyme-catalyzed reactions are gaining significant attention due to their low environmental impact and sustainability. One interesting approach to these reactions is the use of several different cell-free biocatalysts in one-pot (Systems Biocatalysis) which imitates the biosynthetic pathways in living cells. Such cascade reaction is investigated in this work. The first reaction step is the oxidation of amino alcohol catalyzed by alcohol dehydrogenase (ADH) coupled with coenzyme regeneration catalyzed by NADH oxidase (NOX). The second reaction step is the aldol addition of dihydroxyacetone to the oxidation product catalyzed by D-fructose-6-phosphate aldolase (FSA), to synthesize an imino aldol adduct. Our previous experience with similar system showed that such cascade reaction requires careful selection of the reaction conditions to achieve favorable substrate conversion and product yield. Thus, a detailed analysis of the reaction system was done. It included measuring the influence of substrate concentration, coenzyme concentration and ADH/NOX activity ratio on the reaction outcome. Also, enzyme operational stability during the reaction was investigated. At this point the highest diol conversion that was achieved was around 60 % at diol concentration of 20 mM.
Izvorni jezik
Engleski
Znanstvena područja
Kemijsko inženjerstvo, Biotehnologija
POVEZANOST RADA
Projekti:
Horizon 2020 research and innovation programm
grant agreement No 635595
Project CARBAZYMES
Ustanove:
Fakultet kemijskog inženjerstva i tehnologije, Zagreb
Profili:
MORANA ČESNIK KATULIĆ
(autor)
Martina Sudar
(autor)
Zvjezdana Findrik Blažević
(autor)
Đurđa Vasić-Rački
(autor)