| Grant number: | 14/13956-8 |
| Support type: | Scholarships abroad - Research Internship - Post-doctor |
| Effective date (Start): | October 01, 2014 |
| Effective date (End): | September 30, 2015 |
| Field of knowledge: | Biological Sciences - Biochemistry |
| Principal researcher: | Richard John Ward |
| Grantee: | Matheus Pinto Pinheiro |
| Supervisor abroad: | Paul Dupree |
| Home Institution: | Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil |
| Research place: | University of Cambridge, England |
| Associated to the scholarship: | 12/01066-2 - Design of multifunctional enzymes that combine the hydrolysis of B-glucans and Xylans to evaluate the conformation of these polysaccharides in plant cell walls, BP.PD |
Abstract Lignocellulosic biomass, a world-wide abundant renewable feedstock, has a vast potential as renewable carbon source both for biofuel production and in biorefinery. The effective enzymatic hydrolysis of lignocellulosic biomass to monomeric sugars is, however, still hindered by the complexity and inhomogeneous structure of lignocellulosic substrates. The refractory nature of the plant cell wall is due to polysaccharide structures that resist enzymatic attack, and a major challenge for producing cost-effective biofuels and other products is the improvement of enzymatic hydrolytic efficiency of cell wall polysaccharides to fermentable sugars. To achieve this efficiency, a greater knowledge both of the composition and structure of the different biomasses is required in order to develop new enzymes with improved catalytic functions. We are therefore interested in uncovering the architecture of plant cell wall polysaccharides from a variety of renewable feedstocks. The Protein Biochemistry and Biophysics Laboratory at USP-Ribeirão Preto has used advanced protein engineering and synthetic biology methods to design and construct a rigid and elongated polypeptide scaffold based on a beta-prism structure, which allows the fusion of multiple catalytic domains at the prism vertices. We have gone on to create a biocatalyst library where the glycosyl hydrolases (beta-1,4-xylanase and/or beta-1,3-1,4-glucanase) are fused to this scaffold such that the catalytic domains are separated by a range of physical distances and in various defined relative orientations. In the present project, we propose to use this biocatalyst library to assess how the distance and orientation between the catalytic domains influence the profile of released oligosaccharides and, consequently, to probe the polysaccharide architecture in the plant cell walls from sugarcane bagasse, maize and Miscanthus. For this purpose, we intend to employ a novel high throughput method (DNA sequencer-Assisted Saccharide analysis in High throughput - DASH) and software (DASHboard) which has recently been developed in the Dupree Group at the University of Cambridge-UK. The DASH method uses a capillary electrophoresis array (in the form of a DNA sequencing apparatus) to profile fluorescently tagged oligosaccharides derived from enzymatic hydrolysis of plant cell wall polysaccharides. (AU) | |
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