title: Stabilization of D-amino acid oxidase from Rhodosporidium toruloides by immobilization onto magnetic nanoparticles.
abstract: D-amino acid oxidase from Rhodosporidium toruloides was immobilized onto glutaraldehyde-activated magnetic nanoparticles. Approximately four enzyme molecules were attached to one magnetic nanoparticle when the weight ratio of the enzyme to the support was 0.12. After immobilization, the T(m) was increased from 45 degrees C of the free form to 55 degrees C. In the presence of 20 mM H2O2, the immobilized form retained 93% of its activity after 5 h while the free form was completely inactivated after 3.5 h.
authors.affiliation: Department of Bioengineering, Tatung University, 40 Chungshan N. Rd. Sec. 3, Taipei 10452, Taiwan.
authors.forename: Hao-Chieh
authors.initials: HC
authors.lastname: Hsieh
authors.forename: I-Ching
authors.initials: IC
authors.lastname: Kuan
authors.forename: Shiow-Ling
authors.initials: SL
authors.lastname: Lee
authors.forename: Gee-Yeng
authors.initials: GY
authors.lastname: Tien
authors.forename: Yi-Jen
authors.initials: YJ
authors.lastname: Wang
authors.forename: Chi-Yang
authors.initials: CY
authors.lastname: Yu
mesh_terms: D001487:Basidiomycota / Q000201:enzymology*; D003605:D-Amino-Acid Oxidase / Q000737:chemistry* / Q000378:metabolism; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D008280:Magnetics; D053758:Nanoparticles; D013696:Temperature; D013997:Time Factors
chemical_list: D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D006861:Hydrogen Peroxide; D003605:D-Amino-Acid Oxidase