Multicopper Oxidase-Catalyzed Biotransformation of Dihydroquercetin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-09

AUTHORS

M. E. Khlupova, I. S. Vasil’eva, G. P. Shumakovich, O. V. Morozova, E. A. Zaitseva, V. A. Chertkov, A. K. Shestakova, A. V. Kisin, A. I. Yaropolov

ABSTRACT

Multicopper oxidases such as bilirubin oxidase (BOD) from Myrothecium verrucaria and laccase (LC) from the basidial fungus Trametes hirsuta have been used as catalysts in dihydroquercetin (DHQ) oxidative polymerization. The conditions selected enabled good yields of DHQ oligomers, which were then analyzed using UV-vis, FTIR, 1Н and 13С NMR spectroscopy. DHQ oligomers synthesized using both enzymes showed higher thermostability as compared with the monomer. Depending on the oxidase, the products of DHQ polymerization differed in physicochemical properties, and as shown by NMR studies, had different structures. More... »

PAGES

237-243

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http://scigraph.springernature.com/pub.10.3103/s002713141805005x

DOI

http://dx.doi.org/10.3103/s002713141805005x

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