Lipases (triacylglycerol ester hydrolase, EC 3.1.1.3) are enzymes that catalyze the total or partial hydrolysis of fats and oils, releasing free fatty acids, diacylglycerols, monoacylglycerols, and glycerol. Lipases are ubiquitous in nature and are produced by plants, animals and microorganisms. However, microbial lipases, native or recombinant, are the most used in different biotechnological applications. This study aimed to evaluate the production of lipases by a new strain of Pseudomonas sp. using fermentation medium containing byproducts of industrialization of poultry meat or soybean oil. The results indicate that the chicken fat and soybean gum induced 48.3 U/mL and 93.3 U/ml lipase activity, respectively. However, the higher lipase production was obtained when the crude lecithin gum was used, archiving 272.6 U/ml of enzyme activity after 24 hours. The partial biochemical characterization of the enzyme showed that the optimum reaction conditions were pH 9.0 and 35°C. The enzyme was stable at temperatures between 25 to 75 °C and at pH from 6 to 9. At pH 4 and pH 5 absence or reduced activity was observed. The enzyme showed good stability in organic solvents such as acetronitrile, hexane, ethanol and isopropanol. This study indicates that the byproducts tested are promising for the production of lipase and can contribute to the reduction of enzymatic production costs on a large scale, increase the value of these byproducts and reduce potential environmental impacts caused by its accumulation in nature. In addition, lipase from Pseudomonas sp. is stable in a wide range of temperatures and pH and has good stability in organic solvents. Furthermore, it can be used for biodiesel synthesis, biopolymers and production of pharmaceuticals, agrochemicals and fragrances and cosmetics.