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目的探讨氨基功能化磁性纳米粒子的制备及固定α-淀粉酶的效果。方法通过化学共沉淀法制备四氧化三铁磁性纳米粒子,用正硅酸乙酯(TEOS)水解的二氧化硅包裹纳米粒子,并与3-氨丙基三乙氧基硅烷(APTS)发生硅烷化反应进行表面改性功能化修饰,用修饰后的磁性纳米粒子对来源于人唾液的α-淀粉酶进行固定化。结果透射电镜(TEM)显示四氧化三铁磁性纳米粒子形貌均匀;傅里叶变换红外光谱(FTIR)显示四氧化三铁磁性纳米粒子被包裹上二氧化硅和修饰上氨基;固定化后的α-淀粉酶的最大活力是826 U/mg,为游离酶的75%,重复使用7次后活性仍然较高,对pH的稳定性较游离酶增强。结论四氧化三铁磁性纳米粒子可以成功固定α-淀粉酶,固定化后的α-淀粉酶操作的稳定性和重复利用率得到显著提高,为利用其磁性快速分离α-淀粉酶底物提供了可能性。
Objective To investigate the preparation of amino-functionalized magnetic nanoparticles and the effect of immobilizing α-amylase. Methods The ferroferric oxide nanoparticles were prepared by chemical coprecipitation method. The nanoparticles were hydrolyzed by TEOS and encapsulated with 3-aminopropyltriethoxysilane (APTS) The chemical reaction is surface-modified and functionalized, and the human-saliva-derived α-amylase is immobilized with the modified magnetic nano-particles. Results Transmission electron microscope (TEM) showed that the morphology of magnetic nanoparticles was uniform. FTIR showed that the magnetic nanoparticles were coated with silica and modified amino groups. After immobilization The maximum activity of α-amylase is 826 U / mg, which is 75% of the free enzyme. After repeated use for 7 times, the activity is still high, and the stability of the pH is more stable than that of the free enzyme. Conclusions Ferroferric oxide nanoparticles can successfully immobilize α-amylase. The stability and reusability of the immobilized α-amylase can be significantly improved. This provides a rapid magnetic separation of α-amylase possibility.