Izvorni znanstveni članak
https://doi.org/10.15255/CABEQ.2015.2189
Stabilization of D-Amino Acid Oxidase via Covalent Immobilization and Mathematical Model of D-Methionine Oxidative Deamination Catalyzed by Immobilized Enzyme
Z. Findrik
orcid.org/0000-0002-5312-8951
; Faculty of Chemical Engineering and Technology, University of Zagreb, Savska c. 16, HR–10 000 Zagreb, Croatia
M. Tusić
; Pliva Croatia Ltd. Prudnička cesta 98, 10291 Prigorje Brdovečko, Croatia (current position)
Đ. Vasić-Rački
; Faculty of Chemical Engineering and Technology, University of Zagreb, Savska c. 16, HR–10 000 Zagreb, Croatia
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 focus of this work was to evaluate 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.
Ključne riječi
amino acid oxidase; enzyme immobilization; enzyme kinetics; mathematical model
Hrčak ID:
155617
URI
Datum izdavanja:
13.4.2016.
Posjeta: 1.088 *