| Two kinds of macroporous poly(GMA-ST) were synthesized by bulk copolymerization using different pore-forming agents, one only with liquid porogenic agent including cyclohexanol and lauryl alcohol and the other simultaneously with a mixture of cylohexanol, lauryl alcohol and nano-calcium carbonate. After the polymer was smashed, particles with diameters ranging 0.15mm to 0.30mm were taken as the carrier. Scanning electron microscopy (SEM) micrographs were done to character its surface structure. Under the optimum conditions,β-galactosidase was immobilized on the carrier obtained above, the enzyme activity, the activity yield and the basic properties of the immobilized enzyme were determined separately, and satisfactory results were obtained in enzyme activity, activity yield, pH stability, thermal stability, and operational stability. The conclusion obtained indicated that the activity of the immobilized enzyme? on? the ploy(GMA-ST) prepared concurrently with liquid and solid porogen reached a maximum of 535.11U/g dry carrier. So it was more suitable to immobilize enzyme than that purely with liquid solution as pore-forming agents.Macroporous poly(GMA-ST) particles were synthesized via suspension polymerization, with a mixture of cyclohexanol, lauryl alcohol and nano-calcium carbonate as pore-forming agents. SEM micrographs were also done to character its surface structure. Under the optimum conditions,β-galactosidase was immobilized on the carrier obtained above, and the properties of the immobilizedβ-galactosidase were determined. The result showed that the carrier obtained by suspension polymerization was more suitable to immobilize enzyme than that obtained by bulk copolymerization.Novel magnetic beads were prepared from glycidylmethacrylate and styrene via suspension polymerization with cyclohexanol and lauryl alcohol as porogenic agent. The magnetic poly(GMA-ST) beads were characterized with SEM, magnetic scales and X-ray spectroscopy. The magnetic susceptibility of the magnetic poly(GMA-ST) beads was 1.25×10-4cm3/g. Under the optimum conditions, theβ-galactosidase was immobilized on the magnetic poly(GMA-ST) beads. The activity of the immobilizedβ-galactosidase reached 412.09 U/g. It was more suitable to immobilize enzyme than non-magnetic carrier. However, the basic properties of the immobilized enzyme were determined separately, and satisfactory results obtained in pH stability, thermal stability and operational stability. Finally, the values of Michaelis constants Km was also determined.
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