Mechanism of .beta.-aryl ether dimeric lignin model compound oxidation by lignin peroxidase by Phanerochaete chrysosporium

Biochemistry ◽  
1986 ◽  
Vol 25 (17) ◽  
pp. 4790-4796 ◽  
Author(s):  
Keiji Miki ◽  
V. Renganathan ◽  
Michael H. Gold
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Model Compound ◽  
Aryl Ether ◽  
Lignin Model Compound ◽  
Lignin Model

scholarly journals Aromatic–hydroxyl interaction of an alpha-aryl ether lignin model-compound on SBA-15, present at pyrolysis temperatures

2014 ◽  
Vol 16 (44) ◽  
pp. 24188-24193 ◽  
Author(s):  
M. V. Kandziolka ◽  
M. K. Kidder ◽  
L. Gill ◽  
Z. Wu ◽  
A. Savara
Keyword(s):  
Hydrogen Bonds ◽  
Model Compound ◽  
Vibrational Frequencies ◽  
Aryl Ether ◽  
Lignin Model Compound ◽  
Surface Hydroxyls ◽  
Lignin Model

BPEa hydrogen bonds to SBA-15 surface hydroxylsviaan aromatic–hydroxyl interaction characterized by a redshift of >100 cm−1in the OH and CH vibrational frequencies. Surprisingly, this aromatic–hydroxyl interaction is present until ∼400 °C.

scholarly journals A Novel Polyphenol Oxidoreductase OhLac from Ochrobactrum sp. J10 for Lignin Degradation

2021 ◽  
Vol 12 ◽  
Author(s):  
Chenxian Yang ◽  
Lingling Ma ◽  
Xin Wang ◽  
Yuqi Xing ◽  
Xin Lü
Keyword(s):  
Lignin Degradation ◽  
Model Compound ◽  
Corn Stalk ◽  
Aryl Ether ◽  
Docking Analysis ◽  
Lignin Valorization ◽  
Lignin Model Compound ◽  
Effects Of Ph ◽  
Lignin Model ◽  
Chemical Products

Identifying the enzymes involved in lignin degradation by bacteria is important in studying lignin valorization to produce renewable chemical products. In this paper, the catalytic oxidation of lignin by a novel multi-copper polyphenol oxidoreductase (OhLac) from the lignin degrader Ochrobactrum sp. J10 was explored. Following its expression, reconstitution, and purification, a recombinant enzyme OhLac was obtained. The OhLac enzyme was characterized kinetically against a range of substrates, including ABTS, guaiacol, and 2,6-DMP. Moreover, the effects of pH, temperature, and Cu2+ on OhLac activity and stability were determined. Gas chromatography-mass spectrometer (GC-MS) results indicated that the β-aryl ether lignin model compound guaiacylglycerol-β-guaiacyl ether (GGE) was oxidized by OhLac to generate guaiacol and vanillic acid. Molecular docking analysis of GGE and OhLac was then used to examine the significant amino residues and hydrogen bonding sites in the substrate–enzyme interaction. Altogether, we were able to investigate the mechanisms involved in lignin degradation. The breakdown of the lignocellulose materials wheat straw, corn stalk, and switchgrass by the recombinant OhLac was observed over 3 days, and the degradation results revealed that OhLac plays a key role in lignin degradation.

scholarly journals Oxidation of a Tetrameric Nonphenolic Lignin Model Compound by Lignin Peroxidase

2001 ◽  
Vol 276 (25) ◽  
pp. 22985-22990 ◽  
Author(s):  
Tünde Mester ◽  
Katia Ambert-Balay ◽  
Simone Ciofi-Baffoni ◽  
Lucia Banci ◽  
A. Daniel Jones ◽  
...  
Keyword(s):  
Lignin Peroxidase ◽  
Model Compound ◽  
Lignin Model Compound ◽  
Lignin Model
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