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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
Multicopper
oxidase-catalyzed biotransformation of dihydroquercitin
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 dihydroquercitin (DHQ) oxidative polymerization. The conditions
selected enabled good yields of DHQ oligomers, which were then analyzed using UV-vis,
FTIR, 1H č 13C NMR
spectroscopy. DHQ oligomers synthesized using both enzymes showed higher
thermostability as compared with the monomer. Depending on the enzyme used, the
products of DHQ polymerization differed in physico-chemical properties, and as
shown by NMR studies, had different structures.
Key words:
biocatalysis, bilirubinoxidase, fungal laccase, dihydroqurcetin (taxifolin),
enzymatic polymerization, NMR investigation.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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