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Mechanistic bases of evolutionary adaptation to temperature and specificity of glycoside hydrolases belonging to novel GH5 subfamilies

Grant number: 16/00740-2
Support Opportunities:Scholarships in Brazil - Doctorate (Direct)
Effective date (Start): April 01, 2016
Effective date (End): September 03, 2020
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal Investigator:Mário Tyago Murakami
Grantee:Rosa Lorizolla Cordeiro
Host Institution: Centro Nacional de Pesquisa em Energia e Materiais (CNPEM). Ministério da Ciência, Tecnologia e Inovação (Brasil). Campinas , SP, Brazil
Associated scholarship(s):18/22192-2 - Ancestral reconstruction of the GH5_18 beta-mannosidase from Bifidobacterium longum, BE.EP.DD


The production of bioactive compounds, alternative chemicals and biofuels from vegetal biomass is considered one of the most promising strategies to replace the current non-renewable petrochemical routes. One of the main challenges faced is the depolymerization of plant cell wall components, such as cellulose and hemicellulose into simple and/or fermentable sugars. The glycoside hydrolase family 5 (GH5) enzymes degrade a broad spectrum of plant cell wall carbohydrates and therefore have great biotechnological potential. However, its 51 subfamilies predicted, 20 of them remain uncharacterized, which creates a lack of information towards all functional diversity present in this family, which is considered one of the largest and main families in the CAZy universe. Three uncharacterized subfamilies, GH5_18, GH5_19 and GH5_42, are phylogenetically close and predicted as mannanases, but they have been identified in organisms living at very distinct temperature ranges. The Bl18 protein was identified in the mesophilic bacterium Bifidobacterium longum; Tv19 protein belongs to the thermophilic archaea Thermoplasma volcanium; and Pt42 protein was identified in the psychrophilic bacterium Psychroflexus torquis. Through a multidisciplinary approach, this project aims to characterize functionally and structurally these three enzymes belonging to GH5 subfamilies whose activities and structural architecture are still unknown. The information generated in this research will be used for a better understanding of the evolution of GH5 enzymes and might be instrumental for rational protein engineering aiming at potential industrial applications in lignocellulosic biomass degradation. (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)
CORDEIRO, ROSA LORIZOLLA; SIQUEIRA PIROLLA, RENAN AUGUSTO; PERSINOTI, GABRIELA FELIX; GOZZO, FABIO CESAR; DE GIUSEPPE, PRISCILA OLIVEIRA; MURAKAMI, MARIO TYAGO. N-glycan Utilization by Bifidobacterium Gut Symbionts Involves a Specialist beta-Mannosidase. Journal of Molecular Biology, v. 431, n. 4, p. 732-747, . (16/00740-2, 15/26982-0)
CORDEIRO, ROSA L.; SANTOS, CAMILA R.; DOMINGUES, MARIANE N.; LIMA, TATIANI B.; PIROLLA, RENAN A. S.; MORAIS, MARIANA A. B.; COLOMBARI, FELIPPE M.; MIYAMOTO, RENAN Y.; PERSINOTI, GABRIELA F.; BORGES, ANTONIO C.; et al. Mechanism of high-mannose N-glycan breakdown and metabolism by Bifidobacterium longum. Nature Chemical Biology, v. N/A, p. 27-pg., . (16/00740-2, 15/26982-0, 17/15340-2)
Academic Publications
(References retrieved automatically from State of São Paulo Research Institutions)
CORDEIRO, Rosa Lorizolla. Molecular basis of the degradation and metabolism of N-glycans by the probiotic bacterium Bifidobacterium longum. 2020. Doctoral Thesis - Universidade Estadual de Campinas (UNICAMP). Instituto de Biologia Campinas, SP.

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