Affiliation:
1. Assistant Professor, Department of Food Science, Rutgers University 65 Dudley, Rd New Brunswick NJ 80901 USA
2. Director of the Center for Gastrointestinal Physiology, New Jersey Institute of Food Nutrition and Health New Brunswick, NJ USA rogers@aesop.rutgers.edu
Abstract
Self-assembly into nanofibers, although a recently harnessed technology exploited in various industrial applications, occurs naturally in food and biological materials. Proteins, such as gelatin, bovine serum albumin, and β-lactoglobulin, as well as polysaccharides including chitin have most commonly been shown to aggregate into nano-fibers when exposed to appropriate acidic and/or ionic environments. These complex environments lead to protein denaturation and unfolding, followed by aggregation via hydrophobic agglomeration due to the exposed hydrophobic core and secondary hydrogen bonding and disulfide interchanges. The electrostatic, hydrophobic and ionic parameters involved in aggregation are extremely well understood in aqueous environments. However, the underlying principles governing self-assembly into fibrillar networks cannot be extrapolated or applied to hydrophobic environments. In hydrophobic environments, such as vegetable oils, low solubility of proteins and most polysaccharides is an impediment to fibril formation. The insolubility of biological macromolecules has turned the attention of researchers to small amphiphilic molecules capable of aggregating to length scales that are in orders of magnitude greater than their molecular size/volume. These molecules are capable of immobilizing oil via surface tension and capillary forces within a continuous three-dimensional gel network.
Publisher
The Royal Society of Chemistry