Development of barley proteins into peptides nanomicelles for encapsulation of hydrophobic bioactive ingredient

As natural polymer materials, barley proteins have been utilized to fabricate nanocarriers to encapsulate and delivery hydrophobic bioactive ingredients. However, as a result of the high proportion of hydrophobic amino acids and structural rigidity, barley protein-based nanocarriers tend to aggregate easily and have a low loading capacity, which greatly limits their application. In the present study, barley proteins were enzymolyzed to fabricate nanomicelles and then applied to encapsulate hydrophobic bioactive ingredient.

Self-assembled barley peptides could be obtained by controllable enzymolysis of barley proteins. The obtained barley peptides could self-assemble into nanomicelles (BPNMs) with a diameter of approximately 90 nm when the concentration was > 2.1 μg mL^-1. Hydrophobic interaction, disulfide bonds and hydrogen bonds were involved in maintaining the structure of BPNMs. Six self-assembled peptides (QQPFPQ, QTPLPQ, QLPQIPE, QPFPQQPQLPH, QPFPQQPPFGL and QPFPQQPPFWQQQ) were identified and they were characterized by alternating arrangement of hydrophobic amino acids and hydrophilic amino acids. Moreover, BPNMs were utilized to encapsulate hydrophobic bioactive ingredient quercetin. When quercetin was encapsulated by BPNMs, its water solubility was significantly increased, being approximately 30-fold higher than free quercetin. Meanwhile, encapsulation of BPNMs could greatly increase quercetin stability. The interaction between BPNMs and quercetin occurred spontaneously, mainly driven by van der Waals forces and hydrogen bonds.

In the present study, BPNMs were successfully developed and could be used as a promising delivery system to improve the water solubility and stability of hydrophobic bioactive ingredients. © 2024 Society of Chemical Industry.