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Design of multifunctional enzymes that combine the hydrolysis of B-glucans and Xylans to evaluate the conformation of these polysaccharides in plant cell walls

Grant number: 12/01066-2
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): May 01, 2012
Effective date (End): April 10, 2016
Field of knowledge:Biological Sciences - Biochemistry
Principal researcher:Richard John Ward
Grantee:Matheus Pinto Pinheiro
Home Institution: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
Associated research grant:10/18850-2 - Identification, characterization and engineering of plant cell wall degrading enzymes, AP.TEM
Associated scholarship(s):14/13956-8 - Investigation of cell wall polysaccharide architecture from different lignocellulosic feedstocks, BE.EP.PD


The biodegradation of lignocellulosic material has been subject of many studies due to its applicability in biotechnological processes of great relevance to the modern world. The use of enzymes in the lignocellulose biodegradation processes has become increasingly common in the pulp and paper industry, food industry and biorefinery for the production of second-generation bioethanol. Despite the great progress already achieved, much lignocellulose waste with high rates of useful polysaccharides is still discarded. This is because there is still a big gap in understanding the complex residual biomass biodegradation process. The development of this project aims to use technologies associated with protein engineering for the design of chimeric enzymes that combine two distinct catalytic domains, which are involved in the hydrolysis of both ²-glucans and Xylans polysaccharides. Due to the abundant presence of these polysaccharides in the cell walls of plant, studies focusing the degradation of these polysaccharides become of great interest for application in industries, especially in the production of second-generation bioethanol. Furthermore, obtaining many multifunctional enzymes with different combinations of the catalytic domains in the same biocatalyst can help to improve the understanding of the complex conformation of these sugars in cell walls of plants. (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)
SILVA, SERGIO BERGAMACHI; PINHEIRO, MATHEUS PINTO; FUZO, CARLOS ALESSANDRO; SILVA, SAMUEL REGHIM; FERREIRA, TATIANE LOPES; LOURENZONI, MARCOS ROBERTO; NONATO, M. CRISTINA; VIEIRA, DAVI SERRADELLA; WARD, RICHARD JOHN. The role of local residue environmental changes in thermostable mutants of the GH11 xylanase from Bacillus subtilis. International Journal of Biological Macromolecules, v. 97, p. 574-584, . (12/01066-2, 10/18850-2)
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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