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Investigation of cell wall polysaccharide architecture from different lignocellulosic feedstocks

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


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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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
PINHEIRO, P. MATHEUS; REIS, A. G. RENATA; DUPREE, PAUL; WARD, J. RICHARD. Plant cell wall architecture guided design of CBM3-GH11 chimeras with enhanced xylanase activity using a tandem repeat left-handed beta-3-prism scaffold. COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL, v. 19, p. 1108-1118, . (12/01066-2, 16/24139-6, 14/13956-8, 14/50884-5)

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