Pregled bibliografske jedinice broj: 395130
Mathematical modeling of the liquefaction process
Mathematical modeling of the liquefaction process // 1st Conference on ˝Applied Biocatalysis˝ and 5th meeting of students and university professors from Maribor and Zagreb, Book of Abstracts / Habulin, Maja ; Primožič, Mateja (ur.).
Maribor: Tiskarna tehniških fakultet Maribor, 2009. str. 22-23 (predavanje, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 395130 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Mathematical modeling of the liquefaction process
Autori
Fulanović, Nika ; Vrsalović Presečki, Ana ; Vasić-Rački, Đurđa
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
1st Conference on ˝Applied Biocatalysis˝ and 5th meeting of students and university professors from Maribor and Zagreb, Book of Abstracts
/ Habulin, Maja ; Primožič, Mateja - Maribor : Tiskarna tehniških fakultet Maribor, 2009, 22-23
ISBN
978-961-248-153-7
Skup
1st Conference on ˝Applied Biocatalysis˝ and 5th meeting of students and university professors from Maribor and Zagreb
Mjesto i datum
Maribor, Slovenija, 26.05.2009. - 27.05.2009
Vrsta sudjelovanja
Predavanje
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
 -amylase; starch hydrolysis. modelling
Sažetak
Enzymatic starch hydrolysis is a two step process: liquefaction and saccharification. During the first step, starch is dissolved in water and partially hydrolyzed with an α -amylase. In the second step, saccharifying enzymes (glucoamylase, pullulanase) transform liquefied starch into final products which can be specific oligosaccharides such as glucose or maltose, or a mixture of hydrolysates named maltodextrins [1]. The first step of starch hydrolysis, i.e. liquefaction process has been studied in this work. Two commercial α -amylases from Bacilllus licheniformis, known as Termamyl and Liquozyme have been used for this purpose. Using the starch as the substrate, the kinetics of both enzymes has been determined at optimal pH and temperature (pH 7, T = 80 °C). Impact of glucose and maltose on the initial reaction rate was also studied. All kinetic data were collected by the initial reaction rate method. Kinetics of both enzymes was described by Michaelis-Menten kinetics with uncompetitive product inhibition. With the estimated kinetic parameters, mathematical models were developed and validated in the repetitive batch and fed-batch reactor. By the action of Termamyl, glucose and maltose yield was 7 % and 12 % respectively. In the hydrolysis catalyzed by Liquozyme the yield of 16 % on glucose and of 22 % on maltose was observed
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