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Improved operational stability of peroxidases by coimmobilization with glucose oxidase
Author(s) -
van de Velde Fred,
Lourenço Nídia D.,
Bakker Martin,
van Rantwijk Fred,
Sheldon Roger A.
Publication year - 2000
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/1097-0290(20000805)69:3<286::aid-bit6>3.0.co;2-r
Subject(s) - thioanisole , peroxidase , hydrogen peroxide , glucose oxidase , chemistry , catalysis , oxidase test , oxygen , biochemistry , organic chemistry , enzyme
The operational stability of peroxidases was considerably enhanced by generating hydrogen peroxide in situ from glucose and oxygen. For example, the total turnover number of microperoxidase‐11 in the oxidation of thioanisole was increased sevenfold compared with that obtained with continuous addition of H 2 O 2 . Coimmobilization of peroxidases with glucose oxidase into polyurethane foams afforded heterogeneous biocatalysts in which the hydrogen peroxide is formed inside the polymeric matrix from glucose and oxygen. The total turnover number of chloroperoxidase in the oxidation of thioanisole and cis ‐2‐heptene was increased to new maxima of 250 · 10 3 and 10 · 10 3 , respectively, upon coimmobilization with glucose oxidase. Soybean peroxidase, which normally shows only classical peroxidase activity, was transformed into an oxygen‐transfer catalyst when coimmobilized with glucose oxidase. The combination catalyst mediated the enantioselective oxidation of thioanisole [50% ee ( S )] with 210 catalyst turnovers. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 69: 286–291, 2000.