RESUMEN
Steroidal hormones such as estriol (E3), are resistant to biodegradation; hence their removal by conventional treatment systems (aerobic and anaerobic) facilities is limited. These substances are detected in surface water, and present risks to the aquatic ecosystem and humans via potential biological activity. Photochemical treatments can be used to remove E3; however, just a few studies have analyzed the kinetics, intermediates, and E3 degradation pathways in natural surface water. In this study, the behavior of E3 under ultraviolet irradiation associated with H2O2, O3 or TiO2 was investigated to determine the degradation potential and the transformation pathways in reactions performed with a natural surface water sample. E3 degradation kinetics (200 ppb) fitted well to the pseudo-first-order kinetics model, with kinetic constant k in the following order: kUV/O3 > kUV/TiO2 > kUV/H2O2 > kUV. The mechanism of degradation using different advanced oxidative processes seemed to be similar and 12 transformation byproducts were identified, with 11 of them being reported here for the first time. The byproducts could be formed by the opening of the aromatic ring and addition of a hydroxyl radical. A possible route of E3 degradation was proposed based on the byproducts identified, and some of the byproducts presented chronic toxicity to aquatic organisms, demonstrating the risks of exposure.
Asunto(s)
Peróxido de Hidrógeno , Agua , Ecosistema , Estriol , Procesos FotoquímicosRESUMEN
This study aimed to evaluate the waste cooking oil (WCO) hydrolysis in ultrasonic system using lipase as catalyst. Lipase was produced by the fungus Aspergillus niger via solid state fermentation (SSF) using canola meal as substrate. Prior to the hydrolysis reaction, the lipase behavior when subjected to ultrasound was evaluated by varying the temperature of the ultrasonic bath, the exposure time and the equipment power. Having optimized the treatment on ultrasound, the WCO hydrolysis reaction was carried out by evaluating the oil:water ratio and the lipase concentration. For a greater homogenization of the reaction medium, a mechanical stirrer at 170rpm was used. All steps were analyzed by experimental design technique. The lipase treatment in ultrasound generated an increase of about 320% in its hydrolytic activity using 50% of ultrasonic power for 25min. at 45°C. The results of the experimental design conducted for ultrasound-assisted hydrolysis showed that the best condition was using an oil:water ratio of 1:3 (v:v) and enzyme concentration of 15% (v/v), generating 62.67µmol/mL of free fatty acids (FFA) in 12h of reaction. Thus, the use of Aspergillus niger lipase as a catalyst for hydrolysis reaction of WCO can be considered as a possible pretreatment technique of the oil in order to accelerate its degradation.
Asunto(s)
Biocatálisis , Culinaria , Lipasa/metabolismo , Aceites/química , Ondas Ultrasónicas , Residuos , Aspergillus niger/enzimología , HidrólisisRESUMEN
This work investigates the continuous production of alkyl esters from soybean fatty acid (FA) charges using immobilized Novozym 435 as catalyst. The experiments were performed in a packed-bed bioreactor evaluating the effects of FA charge to alcohol (methanol and ethanol) molar ratio, from 1:1 to 1:6, substrate flow rate in the range of 0.5-2.5 mL/min and output irradiation power up to 154 W, at fixed temperature of 65 °C, on the reaction conversion. Results showed that almost complete conversions to fatty acids ethyl esters were achieved at mild ultrasonic power (61.6 W), FA to ethanol molar ratio of 1:6, operating temperature (65 °C) and remained nearly constant for long-term reactions without negligible enzyme activity losses.
Asunto(s)
Ácidos Grasos/química , Glycine max/química , Lipasa/química , Sonido , Enzimas Inmovilizadas , Esterificación , Proteínas Fúngicas , CalorRESUMEN
This work investigates the continuous production of fatty acid ethyl esters from soybean oil in compressed fluids, namely carbon dioxide, propane and n-butane, using immobilized Novozym 435 as catalyst. The experiments were performed in a packed-bed bioreactor evaluating the effects of temperature in the range of 30-70 degrees C, from 50 to 150 bar, oil to ethanol molar ratio of 1:6-1:18 and solvent to substrates mass ratio of 4:1-10:1. In contrast to the use of carbon dioxide and n-butane, results showed that lipase-catalyzed alcoholysis in a continuous tubular reactor in compressed propane might be a potential route to biodiesel production as high reaction conversions were achieved at mild temperature (70 degrees C) and pressure (60 bar) conditions in short reaction times.
Asunto(s)
Glycine max/metabolismo , Lipasa/química , Aceites de Plantas/química , Fuentes de Energía Bioeléctrica , Biotecnología/métodos , Butanos/química , Candida/enzimología , Dióxido de Carbono/química , Catálisis , Enzimas Inmovilizadas/química , Ésteres/química , Proteínas Fúngicas , Presión , Propano/química , TemperaturaRESUMEN
AIMS: The objective of this work was to investigate the lipase production by a newly isolated Penicillium sp., using experimental design technique, in submerged fermentation using a medium based on peptone, yeast extract, NaCl and olive oil, as well as to characterize the crude enzymatic extracts obtained. METHODS AND RESULTS: Lipase activity values of 9.5 U ml(-1) in 96 h of fermentation was obtained at the maximized operational conditions of peptone, yeast extract, NaCl and olive oil concentrations (g l(-1)) of 20.0, 5.0, 5.0 and of 10.0 respectively. The partial characterization of crude enzymatic extract obtained by submerged fermentation showed optimum activity at pH range from 4.9 to 5.5 and temperature from 37 degrees C to 42 degrees C. The crude extract maintained its initial activity at freezing temperatures up to 100 days. CONCLUSIONS: A newly isolated strain of Penicillium sp. used in this work yielded good lipase activities compared to the literature. SIGNIFICANCE AND IMPACT OF THE STUDY: The growing interest in lipase production is related to the potential biotechnological applications that these enzymes present. New lipase producers are relevant to finding enzymes with different catalytic properties of commercial interest could be obtained, without using genetically modified organisms (GMO).