详细信息

Degradation of tetrachloroguaiacol by an enzyme embedded in a magnetic composite cage structure of MNPs@ALG@SiO2  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:Degradation of tetrachloroguaiacol by an enzyme embedded in a magnetic composite cage structure of MNPs@ALG@SiO2

作者:Li, Jie[1];Yang, Yuxiang[1,3];Han, Zhiyong[2];Zhao, Min[1];Yuan, Hongming[4];Ni, Chaoying[3]

机构:[1]East China Univ Sci & Technol, Sch Chem & Mol Engn, Shanghai 200237, Peoples R China;[2]Chengdu Univ Technol, State Key Lab Geohazard Prevent & Geoenvironm Pro, Chengdu 610059, Peoples R China;[3]Univ Delaware, Dept Mat Sci & Engn, Newark, DE 19716 USA;[4]Jilin Univ, State Key Lab Inorgan Synth & Preparat Chem, Changchun 130012, Peoples R China

年份:2021

卷号:170

外文期刊名:BIOCHEMICAL ENGINEERING JOURNAL

收录:;EI(收录号:20211310141132);WOS:【SCI-EXPANDED(收录号:WOS:000640023700001)】;

基金:This work was supported by the National Natural Science Foundation of China (20577010, 20971043), and Xiangqiang Pan, Jiangsu Key Laboratory of Advanced Functional Polymer Design and Application, College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, China for CD characterizations; and the Open Project Program of State Key Laboratory of Inorganic Synthesis and Preparative Chemistry, Jilin University.

语种:英文

外文关键词:Host-guest cage structured; MNPs@ALG@SiO2 composite; Embedding immobilized enzyme; Degradation of TeCG

摘要:Entrapment of enzyme in a cage structure of alginate/silica composite gel can maintain the chemical or configurational structures unchanged in the enzyme, providing a promising means of enzyme immobilization. The alginate/silica composite gel can also provide more adsorption sites for the substrate, which is biocompatible and will carry out degradation and adsorption of pollutants within a cage-like structure reactor simultaneously. In this study, we used a magnetic host-guest cage structured MNPs@ALG@SiO2 composite with a specific enzyme embedded as its guest in the host matrix, to enhance its performance. Additionally, its swelling, leakage rate and immobilization conditions were optimized. The magnetic nanoparticles (MNPs) were used to compensate for the ease of collapse of the internal structure of alginic acid, while SiO2 was used to enhance the swelling resistance of the carrier and prevent the degradation of polysaccharides in the natural environment, thereby maintaining the enzyme biological activity and immobilization rate. Finally, the effects on the degradation of tetrachloroguaiacol (TeCG) by the immobilized enzyme embedded in the MNPs@ALG@SiO2 composite were investigated. When the concentration of ALG was 2% and the TEOS concentration was 40 %, the immobilized MNPs@ALG@SiO2 was found to perform the best. The optimum conditions of immobilizing laccase are pH = 5, enzyme concentration 0.4 g/L, adsorption time 12 h and temperature 20 degrees C. The degradation conditions of TeCG are pH = 6, degradation temperature 40 degrees C, degradation time 10 h and the degradation products of TeCG were acetic acid and ethanol according to GC-MS.

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