材料科学
固定化酶
阳离子聚合
化学工程
纤维素
纤维素酶
催化作用
介孔材料
热稳定性
聚合
高分子化学
聚合物
有机化学
化学
酶
复合材料
工程类
作者
Afsaneh Zarei,Farzaneh Alihosseini,Dambarudhar Parida,Rashid Nazir,Sabyasachi Gaan
标识
DOI:10.1021/acsami.1c12263
摘要
A novel conductive nanohydrogel hybrid support was prepared by in situ polymerization of polyaniline nanorods on an electrospun cationic hydrogel of poly(ε-caprolactone) and a cationic phosphine oxide macromolecule. Subsequently, the cellulase enzyme was immobilized on the hybrid support. Field-emission scanning electron microscopy and Brunauer-Emmett-Teller analyses confirmed a mesoporous, rod-like structure with a slit-like pore geometry for the immobilized support and exhibiting a high immobilization capacity and reduced diffusion resistance of the substrate. For comparison, the catalytic activity, storage stability, and reusability of the immobilized and free enzymes were evaluated. The results showed that the immobilized enzymes have higher thermal stability without changes in the optimal pH (5.5) and temperature (55 °C) for enzyme activity. A high immobilization efficiency (96%) was observed for the immobilized cellulose catalysts after optimization of parameters such as the pH, temperature, incubation time, and protein concentration. The immobilized enzyme retained almost 90% of its original activity after 4 weeks of storage and 73% of its original activity after the ninth reuse cycle. These results strongly suggest that the prepared hybrid support has the potential to be used as a support for protein immobilization.
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