983 resultados para PHYTOPATHOGENIC BACTERIUM
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The opportunistic bacterium Proteus mirabilis secretes a metalloprotease, ZapA, considered to be one of its virulence factors due to its IgA-degrading activity. However, the substrate specificity of this enzyme has not yet been fully characterized. In the present study we used fluorescent peptides derived from bioactive peptides and the oxidized ß-chain of insulin to determine the enzyme specificity. The bradykinin- and dynorphin-derived peptides were cleaved at the single bonds Phe-Ser and Phe-Leu, with catalytic efficiencies of 291 and 13 mM/s, respectively. Besides confirming already published cleavage sites, a novel cleavage site was determined for the ß-chain of insulin (Val-Asn). Both the natural and the recombinant enzyme displayed the same broad specificity, demonstrated by the presence of hydrophobic, hydrophilic, charged and uncharged amino acid residues at the scissile bonds. Native IgA, however, was resistant to hydrolysis by ZapA.
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Cyclodextrin glycosyltransferase (CGTase) is an enzyme that produces cyclodextrins from starch by an intramolecular transglycosylation reaction. Cyclodextrins have been shown to have a number of applications in the food, cosmetic, pharmaceutical, and chemical industries. In the current study, the production of CGTase by Paenibacillus campinasensis strain H69-3 was examined in submerged and solid-state fermentations. P. campinasensis strain H69-3 was isolated from the soil, which grows at 45 C, and is a Gram-variable bacterium. Different substrate sources such as wheat bran, soybean bran, soybean extract, cassava solid residue, cassava starch, corn starch, and other combinations were used in the enzyme production. CGTase activity was highest in submerged fermentations with the greatest production observed at 48-72 h. The physical and chemical properties of CGTase were determined from the crude enzyme produced from submerged fermentations. The optimum temperature was found to be 70-75 degrees C, and the activity was stable at 55 degrees C for 1 h. The enzyme displayed two optimum pH values, 5.5 and 9.0 and was found to be stable between a pH of 4.5 and 11.0.
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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The yeasts are microorganisms with great potential for biotechnological applications in diverse areas. The biological control of phytopathogens by yeasts has showed satisfactory results under laboratory conditions, and it has already produced commercial formulations. With this as focus, this work aims to perform in vitro and in vivo evaluations of the action of a Torulaspora globosa yeast strain (1S112), isolated from sugarcane rhizosphere, against the phytopathogenic mold Colletotrichum sublineolum, the causative agent of anthracnose in sorghum. In vitro experiments included the antagonism test in Petri dishes with morphological hyphal evaluation; yeast killer activity; siderophore, volatile compound and hydrolytic enzyme production. In vivo experiments were conducted in greenhouse conditions with a sorghum variety susceptible to C. sublineolum by evaluating the anthracnose disease for 6 weeks. The results indicated that the yeast strain significantly controlled the fungal growth, either in vitro or in vivo. The strain of T. globosa exhibited killer activity against two sensitive strains, which is a novel capacity for this species. The yeast did not produce siderophores, volatile compounds or hydrolytic enzymes, although it has reduced the mycelial growth, resulting in hyphal deformities but not cell death. The yeast controlled the anthracnose disease in sorghum, either inoculated before or after the fungal spores, suggesting that the competition for space and nutrients to dominate the mold and killer toxin production, altering the hyphal morphology, are mechanisms utilized by the yeast in the biocontrol.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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A bacterium isolated from soil contaminated by hydrocarbon was studied and, by biochemical tests and analysis of PCR, the presence of Bacillus pumilus was identified. The production of biosurfactant was optimized, test of oil degradation and antimicrobial activity determination. The results showed that pH 5.0 and 7.0, 72 h of fermentation, sucrose and sugar cane juice (2%) had best yields. The bacterium is able to degrade crude oil and displays bacteriostatic and fungistatic activity. From the analysis of proximate composition of biosurfactant found the presence of biopolymer formed by a lipopolysaccharide-protein complex.
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Cellulose can be obtained from innumerable sources such as cotton, trees, sugar cane bagasse, wood, bacteria, and others. The bacterial cellulose (BC) produced by the Gram-negative acetic-acid bacterium Acetobacter xylinum has several unique properties. This BC is produced as highly hydrated membranes free of lignin and hemicelluloses and has a higher molecular weight and higher crystallinity. Here, the thermal behavior of BC, was compared with those of microcrystalline (MMC) and vegetal cellulose (VC). The kinetic parameters for the thermal decomposition step of the celluloses were determined by the Capela-Ribeiro non-linear isoconversional method. From data for the TG curves in nitrogen atmosphere and at heating rates of 5, 10, and 20 A degrees C/min, the E(alpha) and B(alpha) terms could be determined and consequently the pre-exponential factor A(alpha) as well as the kinetic model g(alpha). The pyrolysis of celluloses followed kinetic model g(alpha) = [-ln(1 - alpha)](1.63) on average, characteristic for Avrami-Erofeev with only small differences in activation energy. The fractional value of n may be related to diffusion-controlled growth, or may arise from the distributions of sizes or shapes of the reactant particles.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)