Difference in enzymatic dehydrogenative polymerization of dilignols using horseradish peroxidase and crude enzyme obtained from Japanese cypress (Chamaecyparis obtusa)
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biomaterials
Link
http://link.springer.com/content/pdf/10.1186/s10086-019-1809-1.pdf
Reference17 articles.
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2. Shigeto J, Itoh Y, Tsutsumi Y, Kondo R (2012) Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L. FEBS J 279:348–357
3. Shigeto J, Kiyonaga Y, Fujita K, Kondo R, Tsutsumi Y (2013) Putaive cationic cell-wall-bound peroxidase homologues in Arabidopsis, AtPrx2, AtPrx25, and AtPrx71, are involved in lignification. J Agric Food Chem 61:3781–3788
4. Hatfield RD, Vermerris W (2001) Lignin formation in plants. The dilemma of linkage specificity. Plant Physiol 126:1351–1357
5. Fournand D, Cathala B, Lapierre C (2003) Initial steps of the peroxidase-catalyzed polymerization of coniferyl alcohol and/or sinapyl aldehyde: capillary zone electrophoresis study of pH effect. Phytochemistry 62(2):139–146
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1. Bonding of Lignin and Coniferyl Alcohol by a Redox Shuttle of Low-Molecular-Weight Lignols in Enzymatic Oxidative Dehydrogenative Polymerization;Biomacromolecules;2024-05-28
2. Reactivity of a benzylic lignin-carbohydrate model compound during enzymatic dehydrogenative polymerisation of coniferyl alcohol;Holzforschung;2021-01-27
3. Incorporation of catechyl monomers into lignins: lignification from the non-phenolic end via Diels–Alder cycloaddition?;Green Chemistry;2021
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