纤维素
热重分析
结晶度
化学
固定化酶
淀粉酶
傅里叶变换红外光谱
离子键合
共价键
色谱法
化学工程
有机化学
酶
结晶学
工程类
离子
作者
Nitin Kumar Verma,Neera Raghav
标识
DOI:10.1016/j.ijbiomac.2022.10.032
摘要
Tremendous potential exists to use cellulose as a support for the immobilization of enzymes. In the current study, cellulose was transformed into cellulose tosylate, and α-Amylase was immobilized using the derivatized polymer. Techniques like Fourier transform infrared, scanning electron microscopy, thermogravimetric analysis, and X-ray diffraction methods were used to characterize the support. The support is a perfect illustration of how both covalent and hydrophobic/ionic types of immobilizations can be experimentally used on support. The support was found to show max degradation at 320.2 °C with 3.2 % residual substance and crystallinity of about 56.6 %. The support presented maximum enzyme loading at the support: enzyme ratio of 1:4. The immobilized enzyme displayed two ideal pH values (about 4.6 and 7) and two ideal temperatures (approximately 60 °C & 40 °C). It was discovered that the immobilized α-amylase could be used easily eight times with 9.9 % residual activity. The findings of this study show that the immobilized cellulose tosylate enzyme has the potential for application in both acidic and neutral pH environments with the best activity for commercial use.
科研通智能强力驱动
Strongly Powered by AbleSci AI