文献类型：期刊文献

英文题名：Cross-linked enzyme-polymer conjugates with excellent stability and detergent-enhanced activity for efficient organophosphate degradation

作者：Cheng, Huan[1];Zhao, Yu-Lian[1];Luo, Xiao-Jing[1];Xu, Dian-Sheng[1];Cao, Xun[2];Xu, Jian-He[1];Dai, Qing[3];Zhang, Xiao-Yan[1];Ge, Jun[2];Bai, Yun-Peng[1]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Tsinghua Univ, Dept Chem Engn, Beijing 100084, Peoples R China;[3]Natl Ctr Nanosci & Technol, CAS Ctr Excellence Nanosci, Div Nanophoton, Beijing 100190, Peoples R China

年份：2018

卷号：5

期号：1

外文期刊名：BIORESOURCES AND BIOPROCESSING

收录：;EI(收录号：20224513085990);WOS:【SCI-EXPANDED(收录号:WOS:000461106800049)】；

基金：This work was financially sponsored by the National Key Research and Development Program of China (2016YFA0204300), National Natural Science Foundation of China (Nos. 21505044, 21536004 and 21506055) and Natural Science Foundation of Shanghai (18ZR1409900).

语种：英文

外文关键词：Organophosphate; Organophosphate hydrolase; Immobilization; Biodegradation; Enzyme-polymer conjugates; Pluronic F127

摘要：Background: Enzymatic biodegradation of organophosphate pesticides (OPs) is a promising technology to remove these toxic compounds. However, its application in industrial washing was restricted by the lack of efficient immobilized enzymes that can work at high temperatures and high pHs in the presence of various detergents. Therefore, it is necessary to develop a simple method to prepare a robust immobilized enzyme for efficient degradation of OPs. Results: An organophosphate hydrolase (OPH),PoOPHM9, was conjugated and immobilized with a commercially available polymer, Pluronic F127. The prepared cross-linked enzyme-polymer conjugate (CLEPC) displayed higher pH stability in the range from 7.0 to 11.0 and a higher optimal temperature (50 degrees C) than that of free PoOPHM9 (30 degrees C). Its half-life and apparent k(cat)/K-M reached 12.8 h at 50 degrees C and 390.3 +/- 7.8 mM(-1) s(-1), respectively, which were even better than that of the traditional cross-linked enzyme aggregates (CLEA, 7.2 h and 10.9 +/- 1.7 mM(-1) s (-1)). The activity of PoOPHM9 CLEPC was further enhanced up to 2.5-fold by the anionic, nonionic and biocompatible detergents, which was first observed. 0.15 mM Malathion was degraded completely by PoOPHM9 CLEPC after activation within 10 min in the presence of 0.1% (w/w) detergents of all types at pH 9.0 and 25 degrees C, demonstrating its capability in degrading OPs at practically relevant conditions. Conclusion: The conjugation of Pluronic F127 in enzyme immobilization could effectively reduce the activity loss of immobilized enzymes and enhance their stability and activity at high temperatures and high pHs. In addition, the activity of CLEPC can be even enhanced in the presence of various detergents. This technology can be extended easily to produce other immobilized polymer-enzyme conjugates due to its simplicity.