Pregled bibliografske jedinice broj: 364150
Mathematical modelling of glucoamylase catalyzed saccharification process
Mathematical modelling of glucoamylase catalyzed saccharification process // 18th International Congress of Chemical and Process Engineering, Summaries 1, Reaction Engineering: Full text on CD-ROM / Novosad, Jan (ur.).
Prag: Process Engineering Publisher, 2008. str. 1-9 (poster, međunarodna recenzija, cjeloviti rad (in extenso), znanstveni)
CROSBI ID: 364150 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Mathematical modelling of glucoamylase catalyzed
saccharification process
Autori
Findrik, Zvjezdana ; Vrsalović Presečki, Ana ; Vasić-Rački, Đurđa
Vrsta, podvrsta i kategorija rada
Radovi u zbornicima skupova, cjeloviti rad (in extenso), znanstveni
Izvornik
18th International Congress of Chemical and Process Engineering, Summaries 1, Reaction Engineering: Full text on CD-ROM
/ Novosad, Jan - Prag : Process Engineering Publisher, 2008, 1-9
ISBN
978-80-02-02048-6
Skup
18th International Congress of Chemical and Process Engineering
Mjesto i datum
Prag, Češka Republika, 24.08.2008. - 28.08.2008
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
glucoamylase ; enzyme kinetics ; reactor
Sažetak
Glucoamylase obtained from Novozyme was used as a catalyst in the reaction of maltose hydrolysis. Several other disaccharides and oligosaccharides were tested as substrates for this enzyme as well. Commercially known as Dextrozyme, this enzyme has pullulanase (along with glucoamylase) in its contents. Pullulanase prevents the reverse reaction according to several authors. Optimal pH and temperature were found for the enzyme activity: pH 5.5 and 40 °C. Under these conditions maltose hydrolysis were carried out in different reactor types. Enzyme kinetics were determined, and mathematical models for each reactor type were developed. Maltose hydrolysis was carried out in the batch, repetitive batch, fed-batch and continuously operated enzyme membrane reactor. Dextrozyme showed good operational stability in all experiments. Enzyme deactivation was not detected during its prolonged use. This was especially showed in the continuously operated enzyme membrane reactor where Dextrozyme was active for more than 35 days with maltose conversion nearly 100 % during the whole time.
Izvorni jezik
Engleski
Znanstvena područja
Kemijsko inženjerstvo, Biotehnologija
POVEZANOST RADA
Projekti:
MZOS-125-1252086-2793 - Biokatalizatori i biotransformacije (Vasić-Rački, Đurđa, MZOS ) ( CroRIS)
Ustanove:
Fakultet kemijskog inženjerstva i tehnologije, Zagreb
Profili:
Đurđa Vasić-Rački
(autor)
Ana Vrsalović Presečki
(autor)
Zvjezdana Findrik Blažević
(autor)