Bacharelado em Ciências Biológicas (Sede)
URI permanente desta comunidadehttps://arandu.ufrpe.br/handle/123456789/5
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APP - Artigo Publicado em Periódico
TAE - Trabalho Apresentado em Evento
TCC - Trabalho de Conclusão de Curso
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Resultados da Pesquisa
Item Potencial biotecnológico do inibidor de tripsina de flores de Moringa oleifera: uma revisão(2021-12-16) Medeiros, Êsdras da Silva; Pontual, Emmanuel Viana; http://lattes.cnpq.br/1777060469196142; http://lattes.cnpq.br/8379001129790219This work provides a review on the applications of the Moringa oleifera flower trypsin inhibitor (MoFTI) as an insecticidal, antiparasitic, antitumor, immunomodulatory and anti-inflammatory agent. MoFTI is a 18.2-kDa protein (Ki against trypsin of 2.4 μM) that killed (LC50 of 0.3 mg/mL) or delayed the development of newly hatched Aedes aegypti larvae and impaired the growth and viability of the larval gut microbiota (MIC of 0.031 mg/mL; MBC of 1.0 mg/mL). It was also reported that MoFTI caused lysis of Trypanosoma cruzi trypomastigotes (LC50 of 41.2 μg/mL). The inhibitor stimulated the release of the inflammatory cytokines TNF-α and INF-γ, the anti-inflammatory cytokine IL-10, and NO by T. cruzi-infected human peripheral blood mononuclear cells (PBMCs) with the advantage of exerts low toxicity to murine peritoneal macrophages and Vero cells, and no toxicity to human PBMCs. It is known that MoFTI antitumor activity involves the reduction of sarcoma 180 tumor weight in mice and the impairment of the vascularization in tumor microenvironment without exerting toxicity to the animals. Also the inhibitor is an anti-inflammatory and immunomodulatory agent because it reduced paddle edema and leukocyte migration to the peritoneal cavity in mice, and modulated levels of NO, pro-inflammatory (TNF-α, IL-6 and IL-17A) and anti-inflammatory (IL-4 and IL-10) cytokines, respectively. The reviewed data implicate MoFTI as an interesting molecule for biotechnological applications, whether due to its insecticidal potential or pharmacological value.Item Produção de proteases por Aspergillus ochraceus URM 604 obtidas por fermentação em estado sólido utilizando farelo de trigo e resíduo de café como substrato(2021-03-03) Santos, Amanda Lucena dos; Porto, Ana Lúcia Figueiredo; Cardoso, Kethylen Barbara Barbosa; http://lattes.cnpq.br/4784303425329040; http://lattes.cnpq.br/4989617783837981; http://lattes.cnpq.br/3697084385877618Proteases are enzymes of great commercial interest, since it has several industrial applications, such as the pharmaceutical, food, beverages and cleaning products. Among the organisms capable of producing these enzymes are filamentous fungi, having as advantages the possibility of secreting enzymes in the extracellular medium and growing on low-cost substrates. The Solid State Fermentation (SSF) is one of the recommended techniques in the cultivation of filamentous fungi, especially because it simulates its natural habitat, favoring their growth. Aiming the importance of proteases and the growing demand of the global market needs, it is necessary to search for new sources and better production methods. Thus, the objective of this research was to produce proteases by the filamentous fungus Aspergillus ochraceus URM 604 under SSF using substrates derived from the agribusiness, in 2³ factorial design. It was investigated the influence of the type of substrate (coffee residue, wheat bran and 1: 1 coffee + wheat bran), amount of substrate (3g, 5g and 7g ) and humidity (20, 40 and 60%) to determine the ideal conditions for protease production. Fermentation took place for 7 days at 30 °C and the metabolic extract was used for further analysis. For biochemical and physical analysis the protein activity, total proteins, temperature and optimal pH of the obtained enzyme were determined. When analyzing the influence of the variables adopted in the 2³ factorial design, only the type of substrate was a significant parameter. The best substrate was wheat bran, which showed a specific enzymatic activity of 218.27 U / mg under 3g of substrate and 60% humidity. The other conditions also showed high results when compared to the literature. The optimum temperature of the enzyme produced was 50°C and the optimum pH was pH 8-9 (alkaline protease). Thus, this research shows that the fungus A. ochraceus URM 604 has biotechnological potential for protease production under SSF using low-cost substrates such as coffee grounds and wheat bran, this being the first report for the species.Item Recuperação e purificação parcial de proteases colagenolíticas de tainha (Mugil liza) usando precipitação e particionamento em sistemas de fases(2020-02-03) Costa, Beatriz de Aquino Marques da; Porto, Ana Lúcia Figueiredo; http://lattes.cnpq.br/4989617783837981; http://lattes.cnpq.br/2650705679652460Proteases play an important role in the field of biotechnology studies, which is why the research for alternative sources is highly desirable. Thus, combining extraction, recovery and purification techniques to alternative sources, such as by-products of the fishery production chain, in order to generate the least possible damage to the aquatic environment is profitable for the global enzyme market. Therefore, the objective of the present work is to partially recover and purify collagenolytic proteases from Mullet (Mugil liza) digestive viscera with potential biotechnological application. For this, the digestive viscera extract (intestine, liverand a mixture of various viscera) was precipitated using ammonium sulfate ((NH4) 2SO4). In addition, the intestinal viscera were submitted to partitioning by an Aqueous Two-Phase System (ATPS) and a Three-Phase Partitioning system (TPP), to evaluate the most beneficial conditions for the purification of collagenolytic proteases. The results obtained demonstrate that, for ammonium sulphate precipitation, the best results of Purification Factor occurred in concentrations of 30-60% for all assessed extracts (intestine, liver and mix); the aqueous two-phase system (PEG/Citrate) carried out with Mullet intestinal viscera extract demonstrates that the conditions: PEG of 8000 g/mol molar mass; 20% concentration of PEG; 15% citrate concentration lead to the highest purification factor. It is also observed that the collagenases tend to migrate to the PEG-rich phase; for the three-phase system (t-butanol / (NH4) 2SO4) the highest recovery rate of collagenolytic protease was observed in the proportion of 1:0.5, obtaining recovery of 240.01% and a purification factorof 2,55. Thus, it is concluded that the tests can be used in the recovery of biomolecules from neglected organic solid waste from the fishing industry.Item Produção, extração, purificação e caracterização de proteases fibrinolíticas produzidas por Streptomyces parvulus DPUA 1573(2021-11-29) Nascimento, Maria Clara do; Bezerra, Raquel Pedrosa; Batista, Juanize Matias da Silva; http://lattes.cnpq.br/6699725036732885; http://lattes.cnpq.br/1466206759539320; http://lattes.cnpq.br/5929405825655717Due to their fibrin degradation potential, fibrinolytic proteases are a promising alternative in the pharmaceutical industry for the treatment of cardiovascular diseases, especially thrombosis. There are several sources of fibrinolytic proteases, however, the microbial sources are the ones that stand out in terms of low cost and high production rates. From their production to application, enzymes need to go through several processes, which sounds negative, making the steps more costly and late. A method capable of overcoming these problems is the aqueous two-phase system (SDFA), a process capable of reducing downstream steps. The objective of this work was to produce, purify and biochemically characterize the fibrinolytic protease produced by Streptomyces parvulus DPUA 1573. The protease was produced by submerged fermentation using agro-industrial waste or co-products. The crude extract that showed the highest enzymatic activity (passion fruit peel flour) was subjected to extraction by SDFA consisting of polyethylene glycol (PEG) and phosphate salts (potassium and sodium), following a 24 plan. After extraction by SDFA, the protease was subjected to purification by gel filtration chromatography, and already purified had its biochemical characterization performed. The protease produced by S. parvulus DPUA 1573 showed fibrinolytic activity of 15.46 U/mL and was able to form a halo of 317.31 mm2 acting on fibrin degradation. In SDFA, the fibrinolytic protease partitioned preferentially to the PEG-rich phase. The best assay selected according to the combination of the highest specific activity index, purification factor and activity yield was 16, composed of PEG 8,000 gmol-1, 17.5 v/v PEG, pH 8.0 and 15 v/v of phosphate salts. The protease activity of the enzyme was highly stimulated in the presence of iron, reaching a 55% increase in activity, and drastically decreased in the presence of the protease inhibitor 2-mercaptoethanol (91%). The optimum temperature and pH for the enzymatic activity were 40ºC and pH 7.0, respectively, keeping the enzyme activity stable between 30ºC and 60ºC and in the pH range from 7.0 to 8.5. Based on the analyzed results, it was seen that S. parvulus DPUA 1573 proved to be a good producer of fibrinolytic proteases, and the PEG/Phosphate aqueous two-phase system proved to be a great alternative for the extraction and pre-purification of fibrinolytic proteases.