Naslov
Oxidation of N-Cbz-ethanolamine catalyzed by alcohol dehydrogenase (ADH)

Autori
Vukoje, Marina ; Valinger, Davor ; Findrik Blažević, Zvjezdana ; Vasić-Rački, Đurđa ; Kurtanjek, Želimir

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
2nd Conference on Applied biocatalysis and 7th Meeting of Students and University Professors from Maribor and Zagreb / Habulin, M. ; Primožič, M. - Maribor : Tehniških Fakultet, 2011

ISBN
978-961-248-298-5

Skup
Conference on Applied biocatalysis (2 ; 2011) ; Meeting of Students and University Professors from Maribor and Zagreb (7 ; 2011)

Mjesto i datum
Maribor, Slovenija, 07.11.2011. - 08.11.2011

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
oxidation; N-Cbz-ethanolamine; aldehyde; alcohol dehydrogenase

Sažetak
Alcohol dehidrogenase (ADH) belongs to a group of oxidoreductases, class of enzymes responsible for reactions of biological oxidation and reduction. ADH catalyzes the reversible oxidation of alcohole to their corresponding aldehydes or ketones [1]. In this work oxidation of protected ethanolamine (N-Cbz-ethanolamine) catalyzed by enzyme alcohol dehydrogenase from Baker’s yeast is presented. Alcohol dehydrogenase was derived from breaking Baker’s yeast cells (Saccharomyces cerevisiae), followed by separation of enzymes, centrifugation, precipitation (ammonium sulphate) and purification by gel filtration chromatography. Ethanolamines have characteristics of amines and alcohols. Possessing amino and hydroxyl group makes them highly reactive so in this work ethanolamine whose amino group was protected by Cbz group was used. The reaction kinetics was determined in the reaction of aldehyde production by the initial reaction rates method. Measurements were performed on spectrophotometer and from derived experimental data kinetic parameters were estimated. It is shown that N-Cbz-ethanolamine inhibits alcohol dehydrogenase as substrate.

Izvorni jezik
Engleski

Znanstvena područja
Biotehnologija

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