Stabilization of d-amino acid oxidase from Rhodosporidium toruloides by encapsulation in polyallylamine-mediated biomimetic silica

d-Amino acid oxidase from Rhodosporidium toruloides (RtDAO) and Fe3O4 magnetic nanoparticles were encapsulated simultaneously within biomimetic silica, as mediated by polyallylamine. The capacity for this enzyme reached 193 mg/g of biomimetic silica when 15 mg/ml RtDAO was used during encapsulation; the average encapsulation efficiency was approximately 74%. The Tm value (the temperature at which 50% of the initial activity was retained after 1 h of incubation) was increased from 44.3 °C of the free RtDAO to 57.7 °C, clearly indicating the thermal stability was improved by encapsulation. In the presence of 50 mM hydrogen peroxide, encapsulated RtDAO had a half-life of 148 min, an approximately 2-fold increase in resistance to hydrogen peroxide as compared to 78-min half-life of the free form. The encapsulation process is simple and can be completed within minutes; besides, the resultant enzymes can be recovered easily under magnetic field. Such preparation of encapsulated d-amino acid oxidase could be exploited for many potential applications.