Covalent Immobilization of Pancreas Porcine Lipase on Aminated Mesoporous Silica
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Abstract:
In this study mesoporous silica gel was activated by epoxy-group and amino-group for covalent immobilization of pancreas porcine lipase (PPL) using water-soluble carbodiimide. At the optimum conditions (molar ratio of EDC to protein 50:1, weight ratio of support to rude enzyme 10:1, pH 6.0 and immobilization time 8h), the maximum enzyme activity (86.67 U/g) was obtained, which was much higher than that of PPL immobilized onto silica gel without modification (33.33 U/g). The immobilization PPLs were also characterized by scanning electron microscopy (SEM) and Fourier transform infrared spectroscopy (FT-IR). Many filiform substances were observed on the surface of enzyme-immobilized support. Moreover, the absorption peak at 1543 cm-1 (amideⅡ) could be seen in the spectra of immobilized PPL, which confirmed that the PPL had been successfully immobilized onto the supports. In addition, the properties of immobilized PPL were studied. The optimum pH of the immobilized PPL was shifted to a more alkaline range, and the optimum temperature was determined to be 5 ℃ higher than that of free enzyme. Meanwhile, the thermal stability of modified PPL was significantly improved.
