Abstract
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.
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