Magnetic polyvinyl alcohol (PVA) microspheres with 8—64 μm in diameter were prepared from PVA by dispersion and copolymerization with Fe3O4 as magnetite.There were more functional groups, such as hydroxyl and carbox...Magnetic polyvinyl alcohol (PVA) microspheres with 8—64 μm in diameter were prepared from PVA by dispersion and copolymerization with Fe3O4 as magnetite.There were more functional groups, such as hydroxyl and carboxyl etc. on the microsphere surface.1,1′-Carbonyldiimidazole (CDI), a carbonylating agent, was used for the activation of hydroxyl groups of PVA, and α-acetolactatedecarboxylase (ALDC) was immobilized onto the magnetic PVA microspheres by covalent bonding through the amino group.The results showed that total activity, protein binding, specific activity and activity retention of the immobilized enzyme were 63293 U·g -1, 72.67 mg·g -1, 870.96 U·mg -1 and 48.71%,respectively.The optimum temperature of immobilization enzyme was 50℃ and the optimum pH was 6.0.Compared with the free enzyme of ALDC, the thermal, operational and pH stability of the immobilized enzyme were improved.After being stored at 4℃, pH 6.0 for 31 days, the immobilized ALDC retained 95.7% of its initial activity which was 8% higher than the free enzyme.展开更多
文摘Magnetic polyvinyl alcohol (PVA) microspheres with 8—64 μm in diameter were prepared from PVA by dispersion and copolymerization with Fe3O4 as magnetite.There were more functional groups, such as hydroxyl and carboxyl etc. on the microsphere surface.1,1′-Carbonyldiimidazole (CDI), a carbonylating agent, was used for the activation of hydroxyl groups of PVA, and α-acetolactatedecarboxylase (ALDC) was immobilized onto the magnetic PVA microspheres by covalent bonding through the amino group.The results showed that total activity, protein binding, specific activity and activity retention of the immobilized enzyme were 63293 U·g -1, 72.67 mg·g -1, 870.96 U·mg -1 and 48.71%,respectively.The optimum temperature of immobilization enzyme was 50℃ and the optimum pH was 6.0.Compared with the free enzyme of ALDC, the thermal, operational and pH stability of the immobilized enzyme were improved.After being stored at 4℃, pH 6.0 for 31 days, the immobilized ALDC retained 95.7% of its initial activity which was 8% higher than the free enzyme.
