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Applied and Environmental Microbiology, July 2004, p. 3954-3959, Vol. 70, No. 7
0099-2240/04/$08.00+0 DOI: 10.1128/AEM.70.7.3954-3959.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Peter J. I. van de Vondervoort,1,
Jens C. Frisvad,3 Robert A. Samson,4 and Jaap Visser1,
Molecular Genetics of Industrial Microorganisms, Wageningen University, 6703 HA Wageningen,1 Microbiology, Utrecht University, 3584 CH Utrecht,2 Centraalbureau voor Schimmelcultures, 3508 AD Utrecht, The Netherlands,4 Mycology Group, Technical University of Denmark, DK-2800 Lyngby, Denmark3
Received 9 January 2004/ Accepted 2 April 2004
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.
Present address: CatchMabs, 6700 AC Wageningen, The Netherlands.
Present address: Laboratory of Phytopathology, Wageningen University, 6700 EE Wageningen, The Netherlands.
Present address: Fungal Genetics and Technology Consultancy, 6700 AJ Wageningen, The Netherlands.
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