Pregled bibliografske jedinice broj: 475181
Mathematical modelling of glucose oxidation catalyzed by glucose oxidase
Mathematical modelling of glucose oxidation catalyzed by glucose oxidase // Applied Biocatalysis, 6th meeting of students and university professors, Book of Abstracts / Vasić-Rački, Đurđa ; Vrsalović Presečki, Ana (ur.).
Zagreb: Pasanec d.o.o., 2010. str. 21-21 (predavanje, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 475181 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Mathematical modelling of glucose oxidation catalyzed by glucose oxidase
Autori
Fulanović, Nika ; Vrsalović Presečki, Ana ; Vasić-Rački, Đurđa
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Applied Biocatalysis, 6th meeting of students and university professors, Book of Abstracts
/ Vasić-Rački, Đurđa ; Vrsalović Presečki, Ana - Zagreb : Pasanec d.o.o., 2010, 21-21
ISBN
978-553-6470-50-1
Skup
Applied Biocatalysis, 6th meeting of students and university professors
Mjesto i datum
Zagreb, Hrvatska, 09.06.2010
Vrsta sudjelovanja
Predavanje
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
glcose oxidase; modelling; gluconic acid
Sažetak
Gluconic acid is produced from glucose through a simple dehydrogenation reaction catalysed by glucose oxidase [1, 2]. Oxidation of the aldehyde group on the C-1 of b-D-glucose to a carboxyl group results in the production of glucono-δ-lactone and hydrogen peroxide. Glucono-δ-lactone is further spontaneously hydrolysed to gluconic acid [3]. Kinetic behaviour of glucose oxidase isolated from Apsergillus niger was investigated. It was determined that enzyme shows maximal activity on pH 5.7 and the temperature of 35°C. On these conditions the gluconic acid production was very poor because of the low oxygen concentration due to its low solubility at higher temperature. Also at pH 5.7 the rate of the spontaneous hydrolysis of glucono-δ-lactone to gluconic acid is relatively low. So beside at optimal condition the kinetics was also investigated at pH 7 and at 30°C. It was found out that enzyme follows the double substrate Michaelis-Menten kinetics and that the gluconic acid acts as a competitive inhibitor. Model was validated in different reactor types. Sufficient amount of oxygen in the reactor was provided by air supply. Deactivation of enzyme was noticed and was described by the first order kinetic. [1] Bankar S.B., Bule M.V., Singhal R.S., Ananthanarayan L., Biotechnology Advances, 2009, 27: 489–501 [2] Singh, O.V., Kumar R., Appl Microbiol Biotechnol, 2007, 75:713–722
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