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 369496
Title A new black Aspergillus species, A. vadensis, is a promising host for homologous and heterologous protein production
Author(s) Vries, R.P. de; Burgers, K.; Vondervoort, P.J.I. van de; Frisvad, J.C.; Samson, R.A.; Visser, J.
Source Applied and Environmental Microbiology 70 (2004)7. - ISSN 0099-2240 - p. 3954 - 3959.
Department(s) Laboratory of Phytopathology
AFSG Staff Departments (WUATV)
Publication type Refereed Article in a scientific journal
Publication year 2004
Keyword(s) filamentous fungi - niger - acid
Abstract A new species of the group of black aspergilli, Aspergillus vadensis, was analyzed for its potential as a host for homologous and heterologous protein production. Unlike the other black aspergilli, this strain does not acidify the culture medium when nitrate is the nitrogen source and only produces very low levels of extracellular proteases, mainly serine metalloproteases. The stability of A. tubingensis feruloyl esterase A (FaeA) was compared upon production in wild-type A. vadensis, A. tubingensis, and an A. niger strain in which the three main protease-encoding genes were disrupted. The production of FaeA in A. vadensis resulted in larger amounts of intact protein than production in A. tubingensis and was similar to production in an A. niger protease disruptant, confirming in vivo the low proteolytic activity of A. vadensis. The protoplast formation and transformation efficiencies of A. vadensis were much higher than those of A. niger. These characteristics make A. vadensis a very promising candidate for homologous, and possibly heterologous, protein production.
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