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Ausra Peciulyte
Researcher at Chalmers University of Technology
Publications - 10
Citations - 232
Ausra Peciulyte is an academic researcher from Chalmers University of Technology. The author has contributed to research in topics: Cellulose & Hydrolysis. The author has an hindex of 7, co-authored 10 publications receiving 181 citations.
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Impact of the supramolecular structure of cellulose on the efficiency of enzymatic hydrolysis
TL;DR: No significant correlations were observed between the yield of conversion and supramolecular characteristics, such as specific surface area (SSA) and lateral fibril dimensions (LFD), contradicting previous explanations of the increasing crystallinity of cellulose during enzymatic hydrolysis.
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Morphology and enzyme production of Trichoderma reesei Rut C-30 are affected by the physical and structural characteristics of cellulosic substrates
TL;DR: Surprisingly, substantial differences in the enzyme profiles were found even though there were minor Differences in the chemical composition between the cellulose-rich substrates.
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Redox processes acidify and decarboxylate steam-pretreated lignocellulosic biomass and are modulated by LPMO and catalase.
Ausra Peciulyte,Louise Samuelsson,Lisbeth Olsson,K. C. McFarland,Jesper Frickmann,Lars Østergård,Rune Halvorsen,Brian R. Scott,Katja Salomon Johansen,Katja Salomon Johansen,Katja Salomon Johansen +10 more
TL;DR: Abiotic redox processes similar to those that occur in natural water-logged environments also affect the saccharification of pretreated lignocellulose.
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Hydrolytic potential of five fungal supernatants to enhance a commercial enzyme cocktail
TL;DR: Supplementing commercial cocktails with enzymes from carefully selected fungi may result in significantly more efficient saccharification of lignocellulosic materials.
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Biochemical evidence of both copper chelation and oxygenase activity at the histidine brace
Søren Brander,István T. Horváth,Johan Ø. Ipsen,Ausra Peciulyte,Lisbeth Olsson,Cristina Hernández-Rollán,Morten H. H. Nørholm,Susanne Mossin,Leila Lo Leggio,Corinna Probst,Dennis J. Thiele,Katja Salomon Johansen,Katja Salomon Johansen +12 more
TL;DR: To understand better the determinants of reactivity, the biochemical and structural properties of a well-described cellulose-specific LPMO from Thermoascus aurantiacus (TaAA9A) is compared with that of CopC from Pseudomonas fluorescens (PfCopC) and with the L PMO-like protein Bim1 from Cryptococcus neoformans.