期刊
RSC ADVANCES
卷 5, 期 65, 页码 52307-52313出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5ra07916k
关键词
-
资金
- National Natural Science Foundation of China [51039001, 513781906, 51408206]
- Program for Changjiang Scholars and Innovative Research Team in University [IRT-13R17]
- Shanghai Tongji Gao Tingyao Environmental Science & Technology Development Foundation (STGEF)
- Fundamental Research Funds for the Central Universities
Laccase, a type of multicopper oxidase, is capable of efficiently degrading lignin. Until now, the molecular basis of laccase interacting with lignin is still poorly understood. Here, five lignin model compounds (2,6-dimethoxyphenol, ferulic acid, guaiacol, sinapic acid and vanillyl alcohol) were selected to demonstrate the key binding mechanisms between Trametes versicolor laccase and lignin. The results showed that the interaction energies of the lignin model compounds with laccase varied widely, which suggested the different molecular efficiencies of laccase in degrading various components of lignin. This was in full agreement with experimental reports. Hydrophobic interactions seemed to be necessary to the interaction of the lignin/lignin model compounds with laccase, while H-bonds were not essential. The molecular basis revealed by this study was helpful in designing highly efficient laccases against lignin waste to achieve environmental protection.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据