Synthesis of dehydrogenation polymer—polyose complexes by peroxidase

Coniferyl alcohol was dehydrogenatively polymerized in the presence of polyoses by the action of peroxidase in the presence of H 2O 2. Binding site analysis of the resulting synthetic dehydrogenation polymer—carbohydrate complexes by 2,3-dichloro-5,6-dicyano-1,4-benzoquinone oxidation indicated that...

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Published inPhytochemistry (Oxford) Vol. 31; no. 4; pp. 1185 - 1190
Main Authors Ohnishi, Jiro, Watanabe, Takashi, Koshijima, Tetsuo
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Ltd 1992
Elsevier
Subjects
Analysis of complex biological substances
Analytical, structural and metabolic biochemistry
binding sites
biochemical pathways
Biological and medical sciences
biosynthesis
carbohydrates
Dehydrogenation polymer
enzyme activity
Fundamental and applied biological sciences. Psychology
lignin
lignin—carbohydrate complex
literature reviews
peroxidase
plant physiology
Plants and fungi
Dehydrogenation polymer
lignin—carbohydrate complex
peroxidase
biosynthesis
Lignin
Synthesis
Enzyme
Dehydrogenation
Peroxidase
Hydrogen Peroxides
Polysaccharide
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Summary:Coniferyl alcohol was dehydrogenatively polymerized in the presence of polyoses by the action of peroxidase in the presence of H 2O 2. Binding site analysis of the resulting synthetic dehydrogenation polymer—carbohydrate complexes by 2,3-dichloro-5,6-dicyano-1,4-benzoquinone oxidation indicated that acetylglucomannan is bound via ether linkages to the synthetic lignin predominantly at C-6 of hexose moieties while glucuronoxylan is linked at C-2 and C-3 positions of the xylan chain in a similar manner.
ISSN:0031-9422
1873-3700
DOI:10.1016/0031-9422(92)80257-F