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Flavin‐grafted poly(vinyl alcohol): Preparation and properties
Author(s) -
Sanjust Enrico,
Cocco Dina,
Curreli Nicoletta,
Rescigno Antonio,
Sollai Francesca,
Bannister Joe Victor
Publication year - 2002
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.10877
Subject(s) - nad+ kinase , flavin group , chemistry , vinyl alcohol , riboflavin , adduct , polymer chemistry , oxidase test , hydrogen peroxide , substrate (aquarium) , alcohol oxidase , oxygen , alcohol , flavin adenine dinucleotide , aldehyde , derivative (finance) , flavoprotein , cofactor , organic chemistry , enzyme , biochemistry , catalysis , biology , polymer , ecology , pichia pastoris , gene , financial economics , economics , recombinant dna
An NAD(P)H oxidase‐like activity was found in semisynthetic flavoadducts, prepared from an aldehyde derivative of riboflavin and commercial poly(vinylalcohol) (PVA), previously grafted with aminopropyl side chains. Both water‐soluble and water‐insoluble beaded preparations were obtained. The products showed a noticeable NAD(P)H oxidase‐like activity, converting the nucleotide substrate to its oxidized counterpart NAD(P) + at the expense of molecular oxygen, the latter being reduced to hydrogen peroxide. In contrast to some “true” β‐NAD(P)H oxidases, the PVA adducts do not require the presence of additional flavin adenine dinucleotide (FAD) to work; some properties of the flavoadducts were studied that make these flavoadducts good candidates for technological applications. © 2002 Wiley Periodicals, Inc. J Appl Polym Sci 85: 2471–2477, 2002