J
Jacques A.E. Benen
Researcher at Wageningen University and Research Centre
Publications - 58
Citations - 4648
Jacques A.E. Benen is an academic researcher from Wageningen University and Research Centre. The author has contributed to research in topics: Aspergillus niger & Pectate lyase. The author has an hindex of 32, co-authored 58 publications receiving 4427 citations. Previous affiliations of Jacques A.E. Benen include University of Georgia.
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Journal ArticleDOI
Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88
Herman Jan Pel,Johannes H. de Winde,Johannes H. de Winde,David B. Archer,Paul S. Dyer,Gerald Hofmann,Peter J. Schaap,Geoffrey Turner,Ronald P. de Vries,Richard Albang,Kaj Albermann,Mikael Rørdam Andersen,Jannick Dyrløv Bendtsen,Jacques A.E. Benen,Marco A. van den Berg,Stefaan Breestraat,Mark X. Caddick,Roland Contreras,Michael Cornell,Pedro M. Coutinho,Etienne Danchin,Alfons J. M. Debets,Peter J. T. Dekker,Piet W.M. van Dijck,Alard Van Dijk,Lubbert Dijkhuizen,Arnold J. M. Driessen,Christophe d'Enfert,Steven Geysens,Coenie Goosen,Gert S.P. Groot,Piet W. J. de Groot,Thomas Guillemette,Bernard Henrissat,Marga Herweijer,Johannes Petrus Theodorus Wilhelmus Van Den Hombergh,Cees A. M. J. J. van den Hondel,René T. J. M. van der Heijden,Rachel M. van der Kaaij,Frans M. Klis,Harrie J. Kools,Christian P. Kubicek,Patricia Ann van Kuyk,Jürgen Lauber,Xin Lu,Marc J. E. C. van der Maarel,Rogier Meulenberg,Hildegard Henna Menke,Martin Mortimer,Jens Nielsen,Stephen G. Oliver,Maurien M.A. Olsthoorn,K. Pal,K. Pal,Noël Nicolaas Maria Elisabeth Van Peij,Arthur F. J. Ram,Ursula Rinas,Johannes Andries Roubos,Cornelis Maria Jacobus Sagt,Monika Schmoll,Jibin Sun,David W. Ussery,János Varga,Wouter Vervecken,Peter J.J. Van De Vondervoort,Holger Wedler,Han A. B. Wösten,An-Ping Zeng,Albert J. J. van Ooyen,Jaap Visser,Hein Stam +70 more
TL;DR: The filamentous fungus Aspergillus niger is widely exploited by the fermentation industry for the production of enzymes and organic acids, particularly citric acid, and the sequenced genome revealed a large number of major facilitator superfamily transporters and fungal zinc binuclear cluster transcription factors.
Journal ArticleDOI
Synergy between enzymes from Aspergillus involved in the degradation of plant cell wall polysaccharides
Ronald P. de Vries,Harry C.M. Kester,Charlotte Horsmans Poulsen,Jacques A.E. Benen,Jaap Visser +4 more
TL;DR: Synergy in the degradation of two plant cell wall polysaccharides, water insoluble pentosan from wheat flour and sugar beet pectin, was studied using several main-chain cleaving and accessory enzymes.
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Necrotizing activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris
TL;DR: In this paper, five Botrytis cinerea endopolygalacturonase enzymes (BcPGs) were individually expressed in Pichia pastoris, purified to homogeneity and biochemically characterized.
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Analysis of pectic epitopes recognised by hybridoma and phage display monoclonal antibodies using defined oligosaccharides, polysaccharides, and enzymatic degradation
William G.T. Willats,Gerrit Limberg,Hans Christian Buchholt,Gert-Jan W. M. van Alebeek,Jacques A.E. Benen,Tove M.I.E. Christensen,Jaap Visser,Alphons G. J. Voragen,Jørn Dalgaard Mikkelsen,J. Paul Knox +9 more
TL;DR: Investigation of the structure of epitopes recognised by anti-pectin monoclonal antibodies found that optimal JIM5 and JIM7 binding occurs where specific but undefined methyl-esterification patterns are present on HG domains, although fully de-esterified HG samples contain sub-optimal J IM5 epitopes.
Journal ArticleDOI
1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis.
Y. van Santen,Jacques A.E. Benen,Klaus-Hasso Schröter,Kor H. Kalk,Sylvie Armand,Jaap Visser,Bauke W. Dijkstra +6 more
TL;DR: The x-ray structure of endopolygalacturonase II of Aspergillus niger is solved and site-directed mutagenesis studies results in a severe reduction of activity, demonstrating that these residues are important for substrate binding and/or catalysis.