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Biomacromolecules. 2013 Aug 12;14(8):2848-56. doi: 10.1021/bm4006886. Epub 2013 Jul 3.

Cationic β-lactoglobulin nanoparticles as a bioavailability enhancer: protein characterization and particle formation.

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  • 1Department of Nutrition and Food Science, University of Maryland, College Park, 20742, United States.


Cationic β-lactoglobulin (CBLG) was developed as a bioavailability enhancer for poorly absorbed bioactives. At most 11 anionic amino acid residues of β-lactoglobulin (BLG) were substituted by ethylenediamine (EDA), resulting in a highly positive surface charge (zeta potential up to 39 mV at pH 7.0) and significantly increased surface hydrophobicity. These changes conferred CBLG with desirable water solubility and improved mucoadhesion by at most 252%, according to quartz crystal microbalance (QCM) study. Furthermore, CBLG inherited the unique resistance to gastric digestion from BLG, while the digestion under simulated intestinal condition was significantly improved. The latter was possibly due to the formation of aspartic acid-EDA conjugates, together with the randomization of protein conformation related with decreased percentage of β-sheet. Compared to BLG, CBLG formed smaller (75-94 nm), more uniform nanoparticles by the acetone-desolvation method. These merits made CBLG a useful material that provides desirable solubility, controlled release, and enhanced absorption to nutraceuticals or drugs.

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