Protein sourced from natural commodities, such as whey protein, will assemble into long, narrow fibril structures during prolonged thermal treatment in molten-globule states. The resulting fibrils have excellent physical properties as structuring elements, such as high rigidity and cross-sectional width on the order of nanometers, which can provide benefits to the strength or permeability of composite materials. Utilization of these fibrils has been limited by their instability to conditions of pH neutrality and higher ionic strength. Recent research has found means to improve the stability of protein fibrils formed from β-lactoglobulin, a component of whey, at pH values above the protein’s isoelectric point via electrostatic interaction with cationic polymers chitosan and polyethylenimine. Turbidity, zeta potential, and atomic force microscopy were used to confirm the improved stability of the fibrils, with image analysis indicating significant increases in both persistence length and contour length of fibrils at pH values above 5. As an example of the utility of fibrils as supportive materials, β-lactoglobulin fibrils deposited on a flat surface were tested for their ability to improve the growth and differentiation of human mesenchymal stem cells (MSCs). Results showed that cell growth and osteogenic differentiation were not inhibited in the presence of fibrils. Furthermore, chitosan-coated fibrils improved adipogenesis of the MSCs by 113% in relation to conventional culturing techniques, indicating a favorable application of these stabilized protein fibrils.<br/>

Improved stability of whey protein fibrils and utility for biomaterial application

253rd National Meeting (2017)

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