Biochemical, structural and functional characterization of an L-amino acid oxidase...
Evaluating the production and efficacy of bacteriocins by potential probiotic bact...
Grant number: | 12/02833-7 |
Support Opportunities: | Scholarships in Brazil - Scientific Initiation |
Start date: | April 01, 2012 |
End date: | December 31, 2012 |
Field of knowledge: | Biological Sciences - Biochemistry - Chemistry of Macromolecules |
Principal Investigator: | Maurício Ventura Mazzi |
Grantee: | Fabiana Letícia Zambon |
Host Institution: | Pró-Reitoria de Pós-Graduação e Pesquisa. Centro Universitário Hermínio Ometto (UNIARARAS). Fundação Hermínio Ometto (FHO). Araras , SP, Brazil |
Abstract Snake venom is composed of complex substances whose chemical composition and characteristics vary between different known species. The toxicity of the venom is due to the presence of enzymes and proteins, and varying concentrations which include: to neurotoxins, cytotoxins, cardiotoxins, and peptides. The L-amino acid oxidases (LAAOs, E.C. 1.4.3.2) are flavoproteins homodiméricas, which contain a Flavin (FAD, Flavin adenine dinucleotídio or FMN, Flavin mononucleótido) as an enzyme cofactor. LAAOs can be found in bacteria, fungi, green algae, some species of plants and animals, including snakes. In snakes, venoms have been described as inducing a series of toxic effects, such as inducing platelet aggregation, hemorrhage, edema, cytotoxicity, and induction of apoptosis, among other effects, in addition to broad-spectrum bactericidal and anti-parasitic activity. The objective of this project is to characterize functionally an L-amino acid oxidase (LAAOcdt) isolated from the venom of snake species Crotalus durissus terrificus. In this study, the enzyme will be evaluated on its ability to induce cytotoxicity on different gram-positive and negative strains deposited at the ATCC. With the results, knowledge about the function of this toxin on biological systems will be expanded to prospective biotechnological applications.(AU) | |
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