[Spectroscopy study of the immobilized cellulase of magnetic nanoparticles Fe3O4].
Fe3O4 magnetic nanoparticles were synthesized by chemical coprecipitation method using ammonia as the precipitator in the present paper. And then cellulase was immobilized on Fe3O4 magnetic nanoparticles via carbodiimide activation, which was testified by FTIR and lots of repeating catalysis experiments. The morphology of nanoparticles immobilized by cellulase was characterized by TEM, and the activity of cellulase was measured by DNS spectrophotometry. The optimum temperature (60 degrees C) and pH value (3.94-5.50) for the catalysis ablility of immobilized cellulose were studied. The result showed that compared with the native enzyme the cellulase immobilized on Fe3O4 magnetic nanoparticles has the advantages of thermal stability, storage stability, and more extensive optimum pH value.
Wang
Mei
M
Department of Chemistry, Tongji University, Shanghai 200092, China.
Song
Fang
F
Wang
Shi-Long
SL
Wu
Qing-Sheng
QS
D002480:Cellulase / Q000737:chemistry*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D052203:Ferrosoferric Oxide / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D053758:Nanoparticles / Q000737:chemistry / Q000648:ultrastructure; D010316:Particle Size; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D004800:Enzymes, Immobilized; D002480:Cellulase; D052203:Ferrosoferric Oxide