Stabilization of D-Amino Acid Oxidase via Covalent Immobilization and Mathematical Model of D-Methionine Oxidative Deamination Catalyzed by Immobilized Enzyme
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Z. Findrik
2016 Chemical and Biochemical Engineering Quarterly  
Prigorje Brdovečko, Croatia (current position) 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
more » ... ygen supply at air-flow rates of 5 and 10 dm 3 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.
doi:10.15255/cabeq.2015.2189 fatcat:tvi4ii3lofaovnympvh5t7fhqi