Int. J. Mol. Sci. 2013, 14(1), 17-29; doi:10.3390/ijms14010017

Characterization of a Polyamine Microsphere and Its Adsorption for Protein

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Received: 31 August 2012; in revised form: 28 November 2012 / Accepted: 10 December 2012 / Published: 20 December 2012
(This article belongs to the Special Issue Enzyme Optimization and Immobilization)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Keywords: polyamine microsphere; characterization; selective adsorption; protein; lipase
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MDPI and ACS Style

Wang, F.; Liu, P.; Nie, T.; Wei, H.; Cui, Z. Characterization of a Polyamine Microsphere and Its Adsorption for Protein. Int. J. Mol. Sci. 2013, 14, 17-29.

AMA Style

Wang F, Liu P, Nie T, Wei H, Cui Z. Characterization of a Polyamine Microsphere and Its Adsorption for Protein. International Journal of Molecular Sciences. 2013; 14(1):17-29.

Chicago/Turabian Style

Wang, Feng; Liu, Pei; Nie, Tingting; Wei, Huixian; Cui, Zhenggang. 2013. "Characterization of a Polyamine Microsphere and Its Adsorption for Protein." Int. J. Mol. Sci. 14, no. 1: 17-29.

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