埃洛石
固定化酶
纳米管
水解
傅里叶变换红外光谱
淀粉酶
淀粉
化学工程
扫描电子显微镜
化学
材料科学
纳米技术
核化学
有机化学
酶
碳纳米管
复合材料
工程类
作者
Gaurav Pandey,Diogos Marcos Munguambe,Maithri Tharmavaram,Deepak Rawtani,Y. K. Agrawal
标识
DOI:10.1016/j.clay.2016.11.034
摘要
Abstract Amylases are a class of hydrolytic enzymes which help in the conversion of starch into reduced sugars. Several solid carriers have been utilized for the immobilization of amylase. The current study focused on the utilization of halloysite nanotubes (Hal nanotubes) for the immobilization of α-amylase post their surface functionalization with APTES. The immobilized enzyme was characterized for its ultrastructure and morphology using TEM which revealed the hollow tubular structure of nanotubes. Chemical characterization of Amylase-Hal nanotubes powder was done by FTIR in which the characteristic reflections of pristine Hal nanotubes and amylase were detected in the spectra for Amylase-Hal nanotubes powder. The thermal and crystalline behavior of the immobilized enzyme was studied using DSC and XRD analysis respectively. Further, the effect of time, pH, temperature and metal ions on the enzymatic activity of immobilized enzyme had also been probed into. The optimum pH and temperature for the immobilized amylase was found to be 7.4 and 40 °C respectively. Slight increase in the enzymatic activity was also found for immobilized amylase as compared to free enzyme in the presence of Cu2 + and Mn2 + ions.
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