Recuperação e purificação parcial de celulases produzidas por Penicillium sp. FSDE 15

• Autor(a) principal: Silva, Lucas Araujo Trajano
• Data de Publicação: 2023
• Tipo de documento: Dissertação
• Idioma: por
• Título da fonte: Biblioteca Digital de Teses e Dissertações da UFPB
• Texto Completo: https://repositorio.ufpb.br/jspui/handle/123456789/31056
• topic: Catalisadores - Enzimas; Fungo filamentoso - Penicillium; Biomassa; Sistemas aquosos bifásicos; Filamentous fungus; Enzymes; Biomass; ATPS; Penicillium; CNPQ::ENGENHARIAS::ENGENHARIA QUIMICA

Enzymes are highly specialized protein molecules that play a crucial role in accelerating chemical reactions in living organisms. They act as catalysts, reducing the activation energy required for a reaction to occur, thereby increasing the speed of metabolic reactions. Enzyme characterization involves analyzing factors such as temperature, pH, and thermostability to understand their properties and functionalities. Both temperature and pH affect their activity, with most enzymes having optimal operating values. Deviations from these parameters can lead to denaturation. This study aimed to characterize the enzymatic complex produced by the fungus Penicillium sp. FSDE 15, obtained from agroindustrial residues such as wheat bran and corn cobs. The research included the analysis of parameters such as temperature and pH, thermal stability, and different pH values for the enzymes CMCase, FPase, and AVICELase. Enzyme purification and concentration were carried out using salts, organic solvents, and aqueous biphasic systems with polyethylene glycol 4000 and citrate buffer. Tests were conducted at various temperatures (from 40 to 90°C) and pH ranges (from 3 to 6). The optimal temperature range found was from 40 to 50°C, decreasing at higher temperatures. In optimal pH assays, values varied between 3 and 4, depending on the activity under study, with enzymes being more active at lower pH values. The use of ethanol as a precipitating solvent for enzymes was viable at a 1:1 v/v ratio, preserving enzyme characteristics. However, higher concentrations of ethanol, acetone, or ammonium salt resulted in gradual denaturation of the enzymes. The enzymes demonstrated stability within specific temperature ranges, from 40 to 70°C, for 120 minutes, and pH ranging from 3 to 6, which is relevant for industrial applications. The partition study in aqueous biphasic systems revealed no statistically significant interference in the concentrations of polyethylene glycol and sodium citrate analyzed, leading to the choice of the aqueous system with the lowest cost for the formation of the biphasic phase. Comparative analysis with previous studies found in the literature confirmed the results and trends observed in this study.