Stabilization of D-amino acid oxidase from Rhodosporidium toruloides by immobilization onto magnetic nanoparticles.
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.
Hsieh
Hao-Chieh
HC
Department of Bioengineering, Tatung University, 40 Chungshan N. Rd. Sec. 3, Taipei 10452, Taiwan.
Kuan
I-Ching
IC
Lee
Shiow-Ling
SL
Tien
Gee-Yeng
GY
Wang
Yi-Jen
YJ
Yu
Chi-Yang
CY
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
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D006861:Hydrogen Peroxide; D003605:D-Amino-Acid Oxidase