Arabinoxylan in Water through SANS: Single-Chain Conformation, Chain Overlap, and Clustering.

Using small-angle neutron scattering (SANS), we examine the structure and conformational behavior of wheat arabinoxylan (AX) prepared at various concentrations in a sodium phosphate aqueous buffer. As for another major hemicellulose, xyloglucan, we observe a small number of large clusters surrounded by AX chains that behave exactly as a polymer in good solvent with a Flory exponent ν = 0.588. The fit of the data at high q-values to a standard worm-like chain model gives the persistence length lp = 45 Å and cross section of the chains 2Rc = 11-12 Å. In addition, using a dedicated modeling approach, we extract from the SANS data at the intermediate q-range the correlation length ξ of the solutions in the semidilute regime. The decay of ξ with concentration follows a scaling law that further confirms the self-avoiding statistical behavior of the AX chains. This first comprehensive study about the properties of water-soluble AX at different length scales may help in the development of products and processes involving AX as a substitute for fossil carbon molecules.

A tripartite carbohydrate-binding module to functionalize cellulose nanocrystals.

The development of protein and microorganism engineering have led to rising expectations of biotechnology in the design of emerging biomaterials, putatively of high interest to reduce our dependence on fossil carbon resources. In this way, cellulose, a renewable carbon based polysaccharide and derived products, displays unique properties used in many industrial applications. Although the functionalization of cellulose is common, it is however limited in terms of number and type of functions. In this work, a Carbohydrate-Binding Module (CBM) was used as a central core to provide a versatile strategy to bring a large diversity of functions to cellulose surfaces. CBM3a from Clostridium thermocellum, which has a high affinity for crystalline cellulose, was flanked through linkers with a streptavidin domain and an azide group introduced through a non-canonical amino acid. Each of these two extra domains was effectively produced and functionalized with a variety of biological and chemical molecules. Structural properties of the resulting tripartite chimeric protein were investigated using molecular modelling approaches, and its potential for the multi-functionalization of cellulose was confirmed experimentally. As a proof of concept, we show that cellulose can be labelled with a fluorescent version of the tripartite protein grafted to magnetic beads and captured using a magnet.