177 resultados para Lipase enzyme


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Pós-graduação em Ciências Biológicas (Microbiologia Aplicada) - IBRC

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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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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Pós-graduação em Ciências Biológicas (Microbiologia Aplicada) - IBRC

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Pós-graduação em Biologia Geral e Aplicada - IBB

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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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A protein extract containing a plant lipase from oleaginous seeds of Pachira aquatica was tested using soybean oil, wastewater from a poultry processing plant, and beef fat particles as substrate. The hydrolysis experiments were carried out at a temperature of 40°C, an incubation time of 90 minutes, and pH 8.0-9.0. The enzyme had the best stability at pH 9.0 and showed good stability in the alkaline range. It was found that P. aquatica lipase was stable in the presence of some commercial laundry detergent formulations, and it retained full activity up to 0.35% in hydrogen peroxide, despite losing activity at higher concentrations. Concerning wastewater, the lipase increased free fatty acids release by 7.4 times and promoted the hydrolysis of approximately 10% of the fats, suggesting that it could be included in a pretreatment stage, especially for vegetable oil degradation.

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This study reports the immobilization of a new lipase isolated from oleaginous seeds of Pachira aquatica, using beads of calcium alginate (Alg) and poly(vinyl alcohol) (PVA). We evaluated the morphology, number of cycles of reuse, optimum temperature, and temperature stability of both immobilization methods compared to the free enzyme. The immobilized enzymes were more stable than the free enzyme, keeping 60% of the original activity after 4 h at 50°C. The immobilized lipase was reused several times, with activity decreasing to approximately 50% after 5 cycles. Both the free and immobilized enzymes were found to be optimally active between 30 and 40°C.

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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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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)