期刊
BIOTECHNOLOGY LETTERS
卷 31, 期 4, 页码 557-563出版社
SPRINGER
DOI: 10.1007/s10529-008-9894-z
关键词
D-Amino acid oxidase; Immobilization; Magnetic nanoparticle; Rhodosporidium toruloides; Stabilization
资金
- Tatung University [B96-S05-061]
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 45A degrees C of the free form to 55A 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.
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