文献类型：期刊文献

英文题名：Laccase-immobilized tannic acid-mediated surface modification of halloysite nanotubes for efficient bisphenol-A degradation

作者：Zhang, Liting[1,3];Tang, Wen[2];Ma, Tonghao[3];Zhou, Lina[3];Hui, Chenggong[1];Wang, Xiaoli[3];Wang, Ping[4];Zhang, Changai[1];Chen, Chao[3]

机构：[1]Zhejiang Univ Sci & Technol, Zhejiang Prov Key Lab Recycling & Ecotreatment Wa, Hangzhou 310023, Zhejiang, Peoples R China;[2]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, New World Inst Biotechnol, 130 Meilong Rd, Shanghai 200237, Peoples R China;[3]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Sch Biotechnol, Biomed Nanotechnol Ctr, Shanghai 200237, Peoples R China;[4]Univ Minnesota, Dept Bioprod & Biosyst Engn, St Paul, MN 55108 USA

年份：2019

卷号：9

期号：67

起止页码：38935

外文期刊名：RSC ADVANCES

收录：;EI(收录号：20195007818487);WOS:【SCI-EXPANDED(收录号:WOS:000501820700003)】；

基金：This work was supported by the Science and Technology Department of Zhejiang Province (2019C02053 and 2017C03010), National Natural Science Foundation of China (21908059, 21636003 and 41907318), Shanghai Sailing Program (19YF1410900), the China Postdoctoral Science Foundation (2019M651419) and the Shanghai "Super Postdoctoral" Incentive Plan. The authors thank Research Center of Analysis and Test of East China University of Science and Technology for the help on the characterizations.

语种：英文

外文关键词：Enzyme activity - Nanotubes - Kaolinite - Addition reactions - Organic acids - Quinone - Flavonoids - Hyaluronic acid - Tannins

摘要：Halloysite nanotubes (HNTs) have been pursued as promising carriers for enzyme immobilization, but the lack of functional groups severely limits their applications. Herein, we reported a simple tannic acid (TA)-mediated surface modification strategy for the fabrication of HNT-based efficient enzyme immobilization supports. Particularly, TA was first self-polymerized and deposited onto the surface of HNTs to form a thin active film via a mussel-inspired method, and the model enzyme laccase was directly conjugated via the Michael addition and/or Schiff base condensation between quinone groups on poly(tannic acid) layer surfaces and exposed amine groups on laccase surfaces. Under the optimum conditions, this newly fabricated support retained good enzyme-loading and activity recovery properties with 197.9 mg protein per gram of support and 55.4% of activity recovery being achieved. In addition, this immobilized laccase was less influenced by pH, temperature, and inhibitor changes and exhibited higher storage stability than free laccases as more than 70% of initial activity was retained by the immobilized laccase, while less than 30% was retained for free laccase after one-month storage at 4 degrees C. Finally, a higher bisphenol-A (BPA) removal efficiency and more reuse cycles were demonstrated for immobilized laccases. As a result, this TA-mediated surface modification is a simple and green method for biological macromolecule immobilization on HNTs in one step.