School of Food and Biological Engineering, Jiangsu University, Zhenjiang, 212013, Jiangsu, China.
School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, 212013, Jiangsu, China.
Bioprocess Biosyst Eng. 2018 Jul;41(7):1051-1060. doi: 10.1007/s00449-018-1934-z. Epub 2018 Apr 13.
Magnetic double-shell hybrid microspheres (FeO@SiO@p(NIPAM-co-GMA)) have been developed as a promising supported substrate for the immobilization of cellulase. Since the surface of the magnetic microspheres not only contains an epoxy group from GMA (glycidyl methacrylate) that can covalently bind to the enzyme, but also has an intelligent temperature response property from NIPAM (N-isopropylacrylamide), the cellulase can be covalently bonded to the magnetic microspheres and have a temperature-sensitive capability. The immobilized cellulase has the recovery ability of cellulase activity after a high-temperature inactivation. The average amount and activity of immobilized enzymes, respectively, was 233 mg g, 57.4 U mg under the optimized conditions. The experimental results show that the immobilized cellulase has a wider catalytic temperature range, better temperature and storage stability. The residual activity still remained about 65.6% of the initial activity after the sixth catalysis run, which indicated that the immobilized enzyme had high reproducibility.
磁性双壳杂交微球（FeO@SiO@p(NIPAM-co-GMA))已被开发为一种有前途的固定化纤维素酶的载体。由于磁性微球的表面不仅含有环氧基团（来自甲基丙烯酸缩水甘油酯 (glycidyl methacrylate)），可以与酶共价结合，而且还具有来自 N-异丙基丙烯酰胺 (N-isopropylacrylamide) 的智能温度响应特性，因此纤维素酶可以与磁性微球共价结合，并具有温度敏感性。固定化纤维素酶在高温失活后具有恢复酶活性的能力。在优化条件下，固定化酶的平均酶量和酶活分别为 233mg g 和 57.4 U mg。实验结果表明，固定化纤维素酶具有更宽的催化温度范围、更好的温度和储存稳定性。经过第六次催化循环后，其残余活性仍保持在初始活性的 65.6%左右，表明固定化酶具有较高的重现性。
