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Bastien Bissaro

Researcher at Norwegian University of Life Sciences

Publications -  51
Citations -  2492

Bastien Bissaro is an academic researcher from Norwegian University of Life Sciences. The author has contributed to research in topics: Medicine & Chemistry. The author has an hindex of 20, co-authored 41 publications receiving 1510 citations. Previous affiliations of Bastien Bissaro include University of Toulouse & Centre national de la recherche scientifique.

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Oxidative cleavage of polysaccharides by monocopper enzymes depends on H2O2.

TL;DR: The use of H2O2 by a monocopper enzyme that is otherwise cofactor-free offers new perspectives regarding the mode of action of copper enzymes, and these findings have implications for the enzymatic conversion of biomass in Nature and in industrial biorefining.
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Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.

TL;DR: Different lignocellulolytic redox systems, enzymatic or not, that depend on fluxes of reactive oxygen species (ROS) are presented and it is suggested that fine-tuning of H2O2 levels and proximity between sites of H1O2 production and consumption are important for fungal biomass conversion.
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Structural diversity of lytic polysaccharide monooxygenases

TL;DR: The number of available LPMO structures has increased rapidly, including the first structure of an enzyme-substrate complex and the insights gained are reviewed below.
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The impact of hydrogen peroxide supply on LPMO activity and overall saccharification efficiency of a commercial cellulase cocktail

TL;DR: The present report shows that the use of small amounts of a liquid bulk chemical, H2O2, provides an alternative to the currently available processes, which likely is cheaper and more easy to control, while giving higher product yields.
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Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases

TL;DR: A careful analysis of literature data describing non-Leloir transglycosylases and their relationship to glycoside hydrolase counterparts is used to clarify the state of the art knowledge and to establish a new rational basis for the engineering of glycosidic hydrolases.