Multicopper Oxidase-Catalyzed Biotransformation of Dihydroquercetin

被引：1

作者：

Khlupova M.E. ^{[1
]}

Vasil’eva I.S. ^{[1
]}

Shumakovich G.P. ^{[1
]}

Morozova O.V. ^{[1
]}

Zaitseva E.A. ^{[2
]}

Chertkov V.A. ^{[3
]}

Shestakova A.K. ^{[4
]}

Kisin A.V. ^{[4
]}

Yaropolov A.I. ^{[1
]}

机构：

[1] Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences, Moscow

[2] Department of Enzymology, Faculty of Chemistry, Moscow State University, Moscow

[3] Department of Organic Chemistry, Faculty of Chemistry, Moscow State University, Moscow

[4] State Research Institute of Chemistry and Technology of Organoelement Compounds, Moscow

来源：

Moscow University Chemistry Bulletin | 2018年 / 73卷 / 5期

关键词：

bilirubinoxidase; biocatalysis; dihydroquercetin; enzymatic polymerization; fungal laccase; NMR investigation;

D O I：

10.3103/S002713141805005X

中图分类号：

学科分类号：

摘要：

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. © 2018, Allerton Press, Inc.

引用

页码：237 / 243

页数：6

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