A
Adolphus P. G. M. van Loon
Researcher at Hoffmann-La Roche
Publications - 23
Citations - 2294
Adolphus P. G. M. van Loon is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Phytase & Aspergillus niger. The author has an hindex of 17, co-authored 23 publications receiving 2200 citations.
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Journal ArticleDOI
Biochemical Characterization of Fungal Phytases (myo-Inositol Hexakisphosphate Phosphohydrolases): Catalytic Properties
Markus Wyss,Roland Brugger,Alexandra Kronenberger,R. Remy,Rachel Fimbel,Gottfried Oesterhelt,Martin Lehmann,Adolphus P. G. M. van Loon +7 more
TL;DR: To extend the biochemical characterization of wild-type phytases, the catalytic properties of a series of fungal phytased, as well as Escherichia coli phytase, were determined and phosphate liberation kinetics were studied in vitro.
Journal ArticleDOI
The consensus concept for thermostability engineering of proteins: further proof of concept
Martin Lehmann,Claudia Loch,Anke Middendorf,Dominik Studer,Søren Flensted Lassen,Luis Pasamontes,Adolphus P. G. M. van Loon,Markus Wyss +7 more
TL;DR: The present findings support the general validity of the consensus concept for thermostability engineering of proteins.
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The Phytase Subfamily of Histidine Acid Phosphatases: Isolation of Genes for Two Novel Phytases from the Fungi Aspergillus Terreus and Myceliophthora Thermophila
TL;DR: Genes encoding novel phytases from two different filamentous fungi, Aspergillus terreus strain 9A-1 and Myceliophthora thermophila, form a novel subclass of the histidine acid phosphatase family.
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Biophysical Characterization of Fungal Phytases (myo-Inositol Hexakisphosphate Phosphohydrolases): Molecular Size, Glycosylation Pattern, and Engineering of Proteolytic Resistance
Markus Wyss,Luis Pasamontes,Arno Friedlein,R. Remy,Michel Tessier,Alexandra Kronenberger,Anke Middendorf,Martin Lehmann,Line Schnoebelen,Urs Röthlisberger,Eric Kusznir,Guido Wahl,Francis Müller,Hans-Werner Lahm,Kurt Vogel,Adolphus P. G. M. van Loon +15 more
TL;DR: Empirical studies of wild-type phytases from six different fungi revealed that cleavage invariably occurred at exposed loops on the surface of the molecule, and engineering of exposed surface loops may be a strategy for improving phytase stability during feed processing and in the digestive tract.
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From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase.
Martin Lehmann,Dirk Kostrewa,Markus Wyss,Roland Brugger,Allan D'Arcy,Luis Pasamontes,Adolphus P. G. M. van Loon +6 more
TL;DR: For fungal phytases apparently an unexpected direct link between protein sequence conservation and protein stability exists, as a first step towards understanding the molecular basis of increased heat resistance.