Homogeneous and highly stable aqueous soy protein (SP) colloids have been facilely prepared at up to 9 % to exhibit amphoteric (4.5 isoelectric point), amphiphilic (41.2 mN/m surface tension), and polyelectrolyte behaviors (+32.4 mV to -39.1 mV ζ-potentials). The colloidal nanoparticulates (6.0 nm thick, 16.4 nm wide) associate into pH-dependent 157 and 233 nm hydrodynamic dimension aggregates at pH 2.2 and 7.1. SP colloidal particulates have been ice-templated to self-assemble into concentration-dependent ultrafine fibrils (230-680 nm at up to 0.1 %) to laminated fibrous structures (1-1.5 mm at 1-9 %) that subsequently selectively disassembled into semi-crystalline 1.2 µm wide and 45-70 µm long microfibrils. These protein microfibrils are excellent amphiphiles, capable of stabilizing both high-internal-phase o/w and w1/o/w2 double emulsions as well as retaining amphiphilicity even with bound hydrophobic and hydrophilic compounds as demonstrated by lipophilic and water-soluble dyes. This approach of processing globular proteins is scalable and offers a facile way to convert the abundant, but highly under-utilized byproducts of food and biofuel into novel and versatile microfibrils for many potential applications.

Amphoteric and amphiphilic soy protein microfibrils and their functional applications

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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