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Sukyai, P; Rezic, T; Lorenz, C; Mueangtoom, K; Lorenz, W; Haltrich, D; Ludwig, R.
(2008): Comparing soluble and co-immobilized catalysts for 2-ketoaldose production by pyranose 2-oxidase and auxiliary enzymes.
J Biotechnol. 2008; 135(3):281-290 FullText FullText_BOKU

The tri-enzyme system pyranose 2-oxidase (P2O), laccase, and catalase was used to study major parameters in the homogeneous and heterogeneous application of a multi-component enzymatic machinery. P2O oxidizes alcloses to 2-ketosugars, which are interesting intermediates in carbohydrate chemistry, and concomitantly reduces oxygen or alternative electron acceptors. The enzyme was immobilized on eleven agarose or acrylic resins using various coupling methods. The binding capacity was determined and an acrylic carrier with the most suitable properties selected for detailed studies. As P2O shows higher turnover numbers with the electron acceptor 1,4-benzoquinone than with oxygen, the use of this alternative electron acceptor was enabled by employing laccase for the continuous reoxidation of hydroquinone. The laccase regeneration system was found to increase the specific productivity up to 3-fold. Catalase was used to disproportionate the formed hydrogen peroxide in close proximity to the oxygen consuming enzymes and applied in different amounts to adjust the hydrogen peroxide concentration, which was found to be the main reason for enzyme deactivation under turnover conditions. in contrast to homogeneous catalysis, the specific productivity of heterogeneous catalysts under the applied experimental conditions was limited primarily by oxygen transfer, an effect significantly reduced by the laccase regeneration system. (C) 2008 Elsevier B.V. All rights reserved.
Authors BOKU Wien:
Haltrich Dietmar
Lorenz Cindy
Ludwig Roland
Rezic Tonci
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Animals -
Carbohydrate Dehydrogenases - metabolism
Catalysis -
Cattle -
Enzymes, Immobilized - metabolism
Ethylene Oxide - metabolism
Ketoses - biosynthesis
Kinetics -
Laccase - metabolism
Microspheres -
Solubility -
Time Factors -

Find related publications in this database (Keywords)
pyranose 2-oxidase
mass-transfer limitation

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