Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 404955
Title Stabilization and immobilization of Trypanosoma brucei ornithine decarboxylase for the biobased production of 1,4-diaminobutane
Author(s) Könst, P.M.; Franssen, M.C.R.; Scott, E.L.; Sanders, J.P.M.
Source Green Chemistry 13 (2011)5. - ISSN 1463-9262 - p. 1167 - 1174.
Department(s) Biobased Chemistry and Technology
Laboratory for Organic Chemistry
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) nitrogen-containing chemicals - rat-liver - ralstonia-eutropha - pseudomonas-putida - escherichia-coli - amino-acids - covalent immobilization - cyanophycin synthetase - recombinant strains - thiol compounds
Abstract Using the biorefinery concept, L-arginine could become widely available from biomass waste streams via the nitrogen storage polypeptide cyanophycin. In our pursuit to develop a route from biobased L-arginine to 1,4-diaminobutane, one of the monomers in nylon-4,6, we were previously successful in the stabilization and immobilization of Bacillus subtilis arginase. In the present study, we investigated the stabilization and immobilization of Trypanosoma brucei ornithine decarboxylase (EC (TbODC) for its application in the decarboxylation of L-ornithine, the final step in the envisioned route towards 1,4-diaminobutane. The stability observed for TbODC in vitro was substantially improved upon addition of dithiothreitol (DTT), which not only has a stabilizing, but also an activating effect. For optimal TbODC performance, the pH should be controlled at pH 8 and the ionic strength should be kept to a minimum. The temperature for optimal productivity is 40 °C. Immobilization of TbODC on Sepabeads EC-HFA was most successful, leading to an almost three-fold improvement in operational stability as compared to the soluble enzyme. Overall, we demonstrated that by optimization of reaction conditions and covalent immobilization the productivity of TbODC was vastly improved, opening up possibilities for its application in the biobased production of 1,4-diaminobutane
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