Sinapyl alcohol-specific peroxidase isoenzyme catalyzes the formation of the dehydrogenative polymer from sinapyl alcohol

Wataru Aoyama, Shinya Sasaki, Shigeki Matsumura, Thoru Mitsunaga, Hirofumi Hirai, Yuji Tsutsumi, Tomoaki Nishida

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41 Citations (Scopus)

Abstract

Two peroxidases, CWPO-A and CWPO-C, were isolated from the cell walls of poplar (Populus alba L.) callus culture. The cationic CWPO-C showed a strong preference for sinapyl alcohol over coniferyl alcohol as substrate. Thus, the monolignol utilization of CWPO-C is unique compared with other peroxidases, including anionic CWPO-A and horseradish peroxidase (HRP). CWPO-C polymerized oligomeric sinapyl alcohol (S-oligo) and sinapyl alcohol, producing a polymer of greater molecular weight. In contrast, HRP, which is specific to coniferyl alcohol, produced sinapyl alcohol dimers, rather than catalyzing polymerization. Adding coniferyl alcohol as a radical mediator in the HRP-mediated reaction did not result in S-oligo polymerization. This report shows that CWPO-C is an isoenzyme specific to sinapyl alcohol that polymerizes oligomeric lignols. Its catalytic activity toward oligomeric lignols may be related to the lignification of angiosperm woody plant cell walls.

Original languageEnglish
Pages (from-to)497-504
Number of pages8
JournalJournal of Wood Science
Volume48
Issue number6
DOIs
Publication statusPublished - Jan 1 2002

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All Science Journal Classification (ASJC) codes

  • Biomaterials

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