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Study and characterization of enzymes catalase and gluthathione peroxidase from Trichoderma reesei

Grant number: 19/05227-0
Support type:Scholarships in Brazil - Scientific Initiation
Effective date (Start): July 01, 2019
Effective date (End): July 31, 2021
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal researcher:Felipe Santiago Chambergo Alcalde
Grantee:Amanda Cristina Esteves Leite
Home Institution: Escola de Artes, Ciências e Humanidades (EACH). Universidade de São Paulo (USP). São Paulo , SP, Brazil


Enzymes are important biological catalysts that play a key role in several economic activities in different sectors of society, such as: medical, food, textile, pharmaceutical, biofuel, animal feed, in cleaning process as part of detergents, diagnostics, chemistry, pulp and paper industry and many others. The global market for enzymes should show a compound annual growth rate (CAGR) of 6.6% between 2016 and 2024, and that market is expected to reach about $ 17.6 billion by 2024 (AmeriResearch Inc, 2017).The antioxidant defense system enzymes: superoxide dismutase (SOD), glutathione peroxidase (GPx) and Catalase (Cat), are the subject of research for use in the various areas of biotechnology. The present proposal aims to express, purify and characterize the glutathione peroxidase (GPx) and Catalase (Cat) enzymes from the filamentous fungus Trichoderma reesei in order to evaluate its biotechnological potential.

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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)
ADRIANI, PATRICIA P.; DE PAIVA, FERNANDA C. R.; DE OLIVEIRA, GABRIEL S.; LEITE, AMANDA C.; SANCHES, ADRIANA S.; LOPES, ADRIANA RIOS; DIAS, MARCIO V. B.; CHAMBERGO, FELIPE S. Structural and functional characterization of the glutathione peroxidase-like thioredoxin peroxidase from the fungus Trichoderma reesei. International Journal of Biological Macromolecules, v. 167, p. 93-100, JAN 15 2021. Web of Science Citations: 0.

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