Generation of lignin polymer models via dehydrogenative polymerization of coniferyl alcohol and syringyl alcohol via several plant peroxidases involved in lignification and analysis of the resulting DHPs by MALDI-TOF analysis

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Abstract

The mechanism of lignin dehydrogenative polymerization (DHP), made by means of horseradish peroxidase (HRP), was studied in comparison with other plant peroxidases. Interestingly, HRP is efficient for guaiacyl type polymer formation (G-DHPs), but is not efficient in the case of syringyl type DHPs (S-DHPs). It was previously demonstrated that lignification-related Arabidopsis thaliana peroxidases, AtPrx2, AtPrx25 and AtPrx71, and cationic cell-wall-bound peroxidase (CWPO-C) from Populus alba are successful to oxidize syringyl- and guaiacyl-type monomers and larger lignin-like molecules. This is the reason why in the present study the DHP formation by means of these recombinant peroxidases was tested, and all these enzymes were successful for formation of both G-DHP and S-DHP in acceptable yields. CWPO-C led to S-DHP molecular size distribution similar to that of isolated lignins.

Original languageEnglish
Pages (from-to)267-274
Number of pages8
JournalHolzforschung
Volume72
Issue number4
DOIs
Publication statusPublished - Mar 28 2018

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Peroxidases
Lignin
Polymers
Alcohols
Polymerization
Horseradish Peroxidase
Peroxidase
Enzymes
Monomers
Molecules
coniferyl alcohol

All Science Journal Classification (ASJC) codes

  • Biomaterials

Cite this

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title = "Generation of lignin polymer models via dehydrogenative polymerization of coniferyl alcohol and syringyl alcohol via several plant peroxidases involved in lignification and analysis of the resulting DHPs by MALDI-TOF analysis",
abstract = "The mechanism of lignin dehydrogenative polymerization (DHP), made by means of horseradish peroxidase (HRP), was studied in comparison with other plant peroxidases. Interestingly, HRP is efficient for guaiacyl type polymer formation (G-DHPs), but is not efficient in the case of syringyl type DHPs (S-DHPs). It was previously demonstrated that lignification-related Arabidopsis thaliana peroxidases, AtPrx2, AtPrx25 and AtPrx71, and cationic cell-wall-bound peroxidase (CWPO-C) from Populus alba are successful to oxidize syringyl- and guaiacyl-type monomers and larger lignin-like molecules. This is the reason why in the present study the DHP formation by means of these recombinant peroxidases was tested, and all these enzymes were successful for formation of both G-DHP and S-DHP in acceptable yields. CWPO-C led to S-DHP molecular size distribution similar to that of isolated lignins.",
author = "Jun Shigeto and Hiroki Honjo and Koki Fujita and Yuji Tsutsumi",
year = "2018",
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T1 - Generation of lignin polymer models via dehydrogenative polymerization of coniferyl alcohol and syringyl alcohol via several plant peroxidases involved in lignification and analysis of the resulting DHPs by MALDI-TOF analysis

AU - Shigeto, Jun

AU - Honjo, Hiroki

AU - Fujita, Koki

AU - Tsutsumi, Yuji

PY - 2018/3/28

Y1 - 2018/3/28

N2 - The mechanism of lignin dehydrogenative polymerization (DHP), made by means of horseradish peroxidase (HRP), was studied in comparison with other plant peroxidases. Interestingly, HRP is efficient for guaiacyl type polymer formation (G-DHPs), but is not efficient in the case of syringyl type DHPs (S-DHPs). It was previously demonstrated that lignification-related Arabidopsis thaliana peroxidases, AtPrx2, AtPrx25 and AtPrx71, and cationic cell-wall-bound peroxidase (CWPO-C) from Populus alba are successful to oxidize syringyl- and guaiacyl-type monomers and larger lignin-like molecules. This is the reason why in the present study the DHP formation by means of these recombinant peroxidases was tested, and all these enzymes were successful for formation of both G-DHP and S-DHP in acceptable yields. CWPO-C led to S-DHP molecular size distribution similar to that of isolated lignins.

AB - The mechanism of lignin dehydrogenative polymerization (DHP), made by means of horseradish peroxidase (HRP), was studied in comparison with other plant peroxidases. Interestingly, HRP is efficient for guaiacyl type polymer formation (G-DHPs), but is not efficient in the case of syringyl type DHPs (S-DHPs). It was previously demonstrated that lignification-related Arabidopsis thaliana peroxidases, AtPrx2, AtPrx25 and AtPrx71, and cationic cell-wall-bound peroxidase (CWPO-C) from Populus alba are successful to oxidize syringyl- and guaiacyl-type monomers and larger lignin-like molecules. This is the reason why in the present study the DHP formation by means of these recombinant peroxidases was tested, and all these enzymes were successful for formation of both G-DHP and S-DHP in acceptable yields. CWPO-C led to S-DHP molecular size distribution similar to that of isolated lignins.

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