Enzymatic hydrolysis at high dry matter content: The influence of the substrates' physical properties and of loading strategies on mixing and energetic consumption.

The present work investigates the impact of the physical properties and loading strategies of wheat straw and miscanthus on enzymatic hydrolysis at high DM concentration. Three parameters have been chosen to evaluate the enzymatic hydrolysis performance: (i) the mixing time, (ii) the energetic mixing consumption and (iii) the glucose concentration. It was demonstrated that the hydrolysis of miscanthus is easy to perform and has low viscosity. On the contrary, the higher porosity grade of wheat straw than miscanthus (73% against 52%) contributed to have a very high viscosity at 20% w/w DM. The development of a fed-batch strategy allowed the reduction of viscosity inducing the energetic consumption lowering from 30 kJ to 10 kJ. It has been also proven that the miscanthus addition in wheat straw achieved to decrease mixing energy consumption at 5-8 kJ, when it represented more than 30% of the total mass of the reaction medium.

Specific and non-specific enzymes for furanosyl-containing conjugates: biosynthesis, metabolism, and chemo-enzymatic synthesis.

There is no doubt now that the synthesis of compounds of varying complexity such as saccharides and derivatives thereof continuously grows with enzymatic methods. This review focuses on recent basic knowledge on enzymes specifically involved in the biosynthesis and degradation of furanosyl-containing polysaccharides and conjugates. Moreover, and when possible, biocatalyzed approaches, alternative to standard synthesis, will be detailed in order to strengthen the high potential of these biocatalysts to go further with the preparation of rare furanosides. Interesting results will be also proposed with chemo-enzymatic processes based on nonfuranosyl-specific enzymes.

Exploring the synthetic potency of the first furanothioglycoligase through original remote activation.

Thioglycosidic bonds are of utmost importance in biomolecules as their incorporation led to more stable glycomimetics with potential drug activities. Until now only chemical methods were available for their incorporation into glycofuranosyl conjugates. Herein, we wish to describe the use of the first furanothioglycoligase for the preparation of a great variety of thioaryl derivatives with moderate to excellent yields. Of great interest, a stable 1-thioimidoyl arabinofuranose, classically used in chemical glycosylation, was able to efficiently act as a donor through an original enzymatic remote activation mechanism. Study of the chemical structure as well as the nucleophilicity of the thiol allowed us to optimize this biocatalyzed process. As a consequence, this mutated enzyme constitutes an original, mild and eco-friendly method of thioligation.