Characterization of a Polyamine Microsphere and Its Adsorption for Protein
Open Access
- 20 December 2012
- journal article
- research article
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 14 (1), 17-29
- https://doi.org/10.3390/ijms14010017
Abstract
A novel polyamine microsphere, prepared from the water-in-oil emulsion of polyethylenimine, was characterized. The investigation of scanning electron microscopy showed that the polyamine microsphere is a regular ball with a smooth surface. The diameter distribution of the microsphere is 0.37–4.29 μm. The isoelectric point of the microsphere is 10.6. The microsphere can adsorb proteins through the co-effect of electrostatic and hydrophobic interactions. Among the proteins tested, the highest value of adsorption of microsphere, 127.8 mg·g−1 microsphere, was obtained with lipase. In comparison with other proteins, the hydrophobic force is more important in promoting the adsorption of lipase. The microsphere can preferentially adsorb lipase from an even mixture of proteins. The optimum temperature and pH for the selective adsorption of lipase by the microsphere was 35 °C and pH 7.0.This publication has 34 references indexed in Scilit:
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