This study aimed to construct a natural peptide-based
emulsion
gel (PG) using small peptides (∼2.2 kDa) by mild enzymatic
hydrolysis of buckwheat proteins. The obtained PG presented a porous
and tight texture and solid–gel viscoelasticity compared with
its parent protein-based emulsion gel. Meanwhile, it exhibited good
resistance against heating and freeze-thawing. Furthermore, peptide–oil
interaction analysis revealed that the gel matrix was enhanced by
the hydrophobic aggregation between peptides and oil molecules, H-bonding
interaction of peptide molecules, and peptide–oil aggregate
repulsion force. Finally, in vitro intestinal digestion experiments
demonstrated that PG could embed and pH-responsively release curcumin
in the gastrointestinal tract at a release rate of 53.9%. The findings
unfold promising opportunities for using natural PG in a range of
applications relying on large proteins or other synthesized molecules.