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 369493
Title Metabolic control analysis of Aspergillus niger L-arabinose catabolism
Author(s) Groot, M.J.L. de; Prathumpai, W.; Visser, J.; Ruijter, G.J.G.
Source Biotechnology Progress 21 (2005)6. - ISSN 8756-7938 - p. 1610 - 1616.
DOI https://doi.org/10.1021/bp050189o
Department(s) Microbiological Laboratory
AFSG Staff Departments (WUATV)
WU Agrotechnology and Food SciencesDepartment of Agrotechnology and Food Sciences
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2005
Keyword(s) alpha-l-arabinofuranosidase - enzyme-catalyzed reactions - d-xylose - extracellular arabinases - degrading enzymes - gene-expression - pichia-stipitis - reductase gene - nidulans - purification
Abstract A mathematical model of the L-arabinose/D-xylose catabolic pathway of Aspergillus niger was constructed based on the kinetic properties of the enzymes. For this purpose L-arabinose reductase, L-arabitol dehydrogenase and D-xylose reductase were purified using dye-affinity chromatography, and their kinetic properties were characterized. For the other enzymes of the pathway the kinetic data were available from the literature. The metabolic model was used to analyze flux and metabolite concentration control of the L-arabinose catabolic pathway. The model demonstrated that flux control does not reside at the enzyme following the intermediate with the highest concentration, L-arabitol, but is distributed over the first three steps in the pathway, preceding and following L-arabitol. Flux control appeared to be strongly dependent on the intracellular L-arabinose concentration. At 5 mM intracellular L-arabinose, a level that resulted in realistic intermediate concentrations in the model, flux control coefficients for L-arabinose reductase, L-arabitol dehydrogenase and L-xylulose reductase were 0.68, 0.17 and 0.14, respectively. The analysis can be used as a guide to identify targets for metabolic engineering aiming at either flux or metabolite level optimization of the L-arabinose catabolic pathway of A. niger. Faster L-arabinose utilization may enhance utilization of readily available organic waste containing hemicelluloses to be converted into industrially interesting metabolites or valuable enzymes or proteins.
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