Pregled bibliografske jedinice broj: 790368
Stabilization of D-amino acid oxidase via covalent immobilization and mathematical model of D-methionine oxidative deamination catalyzed by immobilized enzyme
Stabilization of D-amino acid oxidase via covalent immobilization and mathematical model of D-methionine oxidative deamination catalyzed by immobilized enzyme // Chemical and biochemical engineering quarterly, 30 (2016), 1; 93-102 doi:10.15255/CABEQ.2015.2189 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 790368 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Stabilization of D-amino acid oxidase via covalent
immobilization and mathematical model of
D-methionine oxidative deamination catalyzed by
immobilized enzyme
Autori
Findrik, Zvjezdana ; Tusić, Marko ; Vasić-Rački, Đurđa
Izvornik
Chemical and biochemical engineering quarterly (0352-9568) 30
(2016), 1;
93-102
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
amino acid oxidase ; enzyme immobilization ; enzyme kinetics ; mathematical model
Sažetak
Porcine kidney D-amino acid oxidase was stabilized by covalent immobilization on spherical particles of Eupergit C because of its low stability in soluble form. The main focus of this work was put on evaluation of operational stability of the immobilized enzyme. To evaluate D-amino acid oxidase’s operational stability during process conditions, repetitive batch reactor experiments of D-methionine oxidation reaction were carried out with continuous aeration for oxygen supply at air-flow rates: of 5 and 10 dm3 h-1. Kinetic analysis of the immobilized enzyme was done as well. The mathematical model of D-methionine oxidative deamination catalyzed by the immobilized D-amino acid oxidase was developed and it described the data well. It enabled the estimation of operational stability decay rate constant. It was possible to achieve 100 % substrate conversion in all batch experiments.
Izvorni jezik
Engleski
Znanstvena područja
Kemijsko inženjerstvo, Biotehnologija
POVEZANOST RADA
Ustanove:
Fakultet kemijskog inženjerstva i tehnologije, Zagreb,
PLIVA HRVATSKA d.o.o.
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
Uključenost u ostale bibliografske baze podataka::
- CA Search (Chemical Abstracts)
