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- W4296817114 endingPage "128020" @default.
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- W4296817114 abstract "In order to meet the challenge of enzyme catalysis of waste lignin, laccase (LAC)- guaiacyl(G)-type monomers noncovalent supramolecular system (LGS) were constructed for conversion of lignin. In this contribution, the catalytic effect of LGS formed by LAC and G-type monomers was studied. LAC changes the secondary structure conformation of its binding site to accommodate the G-type monomer, which is bound by hydrogen bonding and hydrophobic interactions. A mechanistic study highlights that the non-covalent complexation accelerates the internal electron transfer rate of LGS and syringol substrate for subsequent coupling reactions. In the presence of guaiacol/4-ethylguaiacol/vanillin-LAC, the conversion of dealkali lignin were 16.44, 29.12 and 22.72, respectively, higher than that in the presence of LAC alone. And the product of syringyl monomer was significantly increased in the actual lignin catalysis. Our work explains the mechanisms underlying existing enzyme-substrate interactions and enhanced catalytic system can be used for efficient utilization of waste." @default.
- W4296817114 created "2022-09-24" @default.
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- W4296817114 date "2022-11-01" @default.
- W4296817114 modified "2023-10-18" @default.
- W4296817114 title "Highly catalytic supramolecular host–guest complex for high value directional conversion of lignin to syringyl monomer" @default.
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- W4296817114 doi "https://doi.org/10.1016/j.biortech.2022.128020" @default.
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