A
Anu Koivula
Researcher at VTT Technical Research Centre of Finland
Publications - 96
Citations - 5824
Anu Koivula is an academic researcher from VTT Technical Research Centre of Finland. The author has contributed to research in topics: Trichoderma reesei & Cellulose. The author has an hindex of 40, co-authored 91 publications receiving 5416 citations. Previous affiliations of Anu Koivula include Uppsala University & Ghent University.
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Journal ArticleDOI
Traffic Jams Reduce Hydrolytic Efficiency of Cellulase on Cellulose Surface
Kiyohiko Igarashi,Takayuki Uchihashi,Anu Koivula,Masahisa Wada,Masahisa Wada,Satoshi Kimura,Satoshi Kimura,Tetsuaki Okamoto,Tetsuaki Okamoto,Merja Penttilä,Toshio Ando,Masahiro Samejima +11 more
TL;DR: The real-time visualization of crystalline cellulose degradation by individual cellulase enzymes through use of an advanced version of high-speed atomic force microscopy is reported here.
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Trichoderma reesei cellobiohydrolases: why so efficient on crystalline cellulose?
TL;DR: 28 Burmeister, W. P., Cottaz, S., Driguez, H., Palmieri, S. and Henrissat, B. (1997) Structure 5, 663-675.
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Crystal Structure of a Laccase from Melanocarpus Albomyces with an Intact Trinuclear Copper Site
Nina Hakulinen,Laura-Leena Kiiskinen,Kristiina Kruus,Markku Saloheimo,Arja Paananen,Anu Koivula,Juha Rouvinen +6 more
TL;DR: The crystal structure of the M. albomyces laccase revealed elongated electron density between all three coppers in the trinuclear copper site, suggesting that an oxygen molecule binds with a novel geometry.
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Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose.
TL;DR: This interaction was used to study the effect of different cellulose-binding domains (CBDs) on the enzymatic activity of C. thermocellum endoglucanase CelD, proving the reversible binding of the intact complexes despite the apparent binding irreversibility of some CBDs.
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High Speed Atomic Force Microscopy Visualizes Processive Movement of Trichoderma reesei Cellobiohydrolase I on Crystalline Cellulose
TL;DR: Real time observations of Trichoderma reesei (Tr) cellobiohydrolase I (Cel7A) molecules sliding on crystalline cellulose are presented with a high speed atomic force microscope and it is indicated that, besides the hydrolysis of glycosidic bonds, the loading of a cellulose chain into the active site tunnel is also essential for the enzyme movement.