Correlation Engine 2.0
Clear Search sequence regions

  • corn (3)
  • enzymes (2)
  • fourier transform (1)
  • gas (1)
  • hydrolysis (2)
  • lignin (16)
  • nitrogen (1)
  • peroxidases (2)
  • zea (1)
  • Sizes of these terms reflect their relevance to your search.

    Lignin of high purity and structural integrity was isolated from the enzymatic residue of corn stover. Degradation of the lignin by laccase, lignin peroxidase, and manganese peroxidase was investigated. Structural changes in the lignin after degradation were characterized by scanning electron microscopy, nitrogen adsorption and Fourier transform infrared spectroscopy, and the enzymatic products were systematically analyzed by gas chromatography mass spectrometry. The highest percentage of lignin degradation was obtained with a mixture of three enzymes (25.79%): laccase (Lac), the starting enzyme of the mixed enzyme reaction, worked with lignin peroxidase (LiP), and manganese peroxidase (MnP) to further degrade lignin. This degradation destroyed the macromolecular structure of lignin, broke its key chemical bonds, and opened benzene rings, thus producing more acidic compounds. This study elucidated the concept of degrading lignin from corn stover using the Lac, LiP and MnP enzymes synergistically, thus providing a theoretical basis for the biodegradation of lignin. Copyright © 2022 Elsevier Ltd. All rights reserved.


    Sitong Zhang, Zijian Dong, Jia Shi, Chengrui Yang, Yi Fang, Guang Chen, Huan Chen, Chunjie Tian. Enzymatic hydrolysis of corn stover lignin by laccase, lignin peroxidase, and manganese peroxidase. Bioresource technology. 2022 Oct;361:127699

    Expand section icon Mesh Tags

    Expand section icon Substances

    PMID: 35905874

    View Full Text