RESUMO
For decades now, low salinity water flooding (LSWF) oil recovery has emerged as an environmentally benign and cost-effective method for improved oil recovery, where research findings have reported pH and interfacial tension effects. Considering the effect of oil chemistry on interfacial tension and the potential of this chemistry to have a direct relationship with LSWF, we measured the interfacial tension of four crude oils with composition varying from those of conventional to unconventional ones. We also characterized the crude oil samples using infrared spectroscopy and a wet chemistry method based on asphaltene precipitation. Our research approach has enabled us to relate the composition of crude oil to the interfacial tension trend at pH encountered in improved oil recovery schemes. Our research methodology, based on an integrated approach to using infrared spectroscopy and interfacial tensiometry, has also enabled us to propose a more robust theoretical explanation for current observations in LSWF related to pH and interfacial tension. In this regard, oil-water interfacial tension depends on the concentration of polar components, such that the higher the concentration of polar groups in crude oil, the higher the interfacial tension at a given pH of aqueous solution. We have also shown that the acid-base behavior of polar groups at the oil-water interface provides a theoretical interpretation of the explicit relationship between oil-water interfacial tension and the electrostatic components of interfacial tension as given by the energy additivity theory.
RESUMO
Peroxidase (EC 1.11.1.7) from horseradish ( Armoracia rusticana ) roots was purified using a simple, rapid, three-step procedure: ultrasonication, ammonium sulfate salt precipitation, and hydrophobic interaction chromatography on phenyl Sepharose CL-4B. The preparation gave an overall yield of 71%, 291-fold purification, and a high specific activity of 772 U mg(-1) protein. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the purified enzyme was homogeneous and had a molecular weight of approximately 40 kDa. The isolated enzyme had an isoelectric point of 8.8 and a Reinheitszahl value of 3.39 and was stable when stored in the presence of glycerol at -20 degrees C, with >95% retention of original enzyme activity for at least 6 months. Maximal activity of purified horseradish peroxidase (HRP) was obtained under different optimized conditions: substrate (guaiacol and H(2)O(2)) concentrations (0.5 and 0.3 mM, respectively), type of buffer (50 mM phosphate buffer), pH (7.0), time (1.0 min), and temperature of incubation (30 degrees C). In addition, the effect of HRP and H(2)O(2) in a neutral-buffered aqueous solution for the oxidation of phenol and 2-chlorophenol substrates was also studied. Different conditions including concentrations of phenol/2-chlorophenol, H(2)O(2), and enzyme, time, pH, and temperature were standardized for the maximal activity of HRP with these substrates; under these optimal conditions 89.6 and 91.4% oxidations of phenol and 2-chlorophenol were obtained, respectively. The data generated from this work could have direct implications in studies on the commercial production of this biotechnologically important enzyme and its stability in different media.
