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Stability of a Lipase Extracted from Seeds of Pachira aquatica in Commercial Detergents and Application Tests in Poultry Wastewater Pretreatment and Fat Particle Hydrolysis

DOI: 10.1155/2013/324061

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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. 1. Introduction Lipases (triacylglycerol lipases, E.C. are enzymes that catalyze the cleavage of carboxyl ester bonds present in acylglycerols with the subsequent release of fatty acids and glycerol. They are particularly important because they specifically hydrolyze oils and fats, an interesting ability for different industrial applications [1]. These enzymes have become more and more prominent on the enzyme biotechnology scenario due to their versatility for hydrolysis and synthesis and for their catalytic reactions often being chemoselective, regionselective, or enantioselective [2]. Lipases can be obtained from animals (pancreatic, hepatic, and gastric sources), microorganisms (bacterial, fungal, and yeast), or plants, with variations in their catalytic properties [3]. Nevertheless, recently, seed lipases have been the focus of increasing attention as biocatalysts. In some cases, these enzymes present advantages over animal and microbial lipases due to some very interesting features such as specificity, low cost, availability, and easily purification, representing a great alternative for potential commercial use as industrial enzymes [4–6]. The participation of lipases in the worldwide enzyme industry market has grown significantly and it includes a wide range of applications in many sectors such as food, pharmaceutical, fine chemical, oil chemical, and detergent industries as well as in biodiesel and wastewater treatment [7–9]. One interesting application of lipases is their use in oil chemical industries, reducing energy expenses and minimizing heat degradation of compounds in comparison to traditional chemical processes [7]. Another potential application is in


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